NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530395903|ref|XP_005253240|]
View 

tripartite motif-containing protein 5 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
 288-489 6.77e-118

PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction.


:

Pssm-ID: 293994  Cd Length: 200  Bit Score: 344.59  E-value: 6.77e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 288 FRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGargtryqtFVNFNYCTGILGSQSITSGKHYWEVDVSK 367
Cdd:cd15822    1 FNELTDVQRYWVHVTLDPSNNKNIVISEDRRQVRYVRKQQRYN--------SNGNNEDYGVLGSPSITSGKHYWEVDVSK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 368 KTAWILGVCAGFQPDAM---------CNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSvpfIVPLSVIICPDRV 438
Cdd:cd15822   73 KRAWILGVCGGKYPNSTlkdfnkqgkNNQKQCSNYQPKYGYWVIGLQNKSEYNAFEDSSSSDPL---ILTLSLTVPPCRV 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 439 GVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15822  150 GVFLDYEAGTVSFFNVTNHGFLIYKFSSCSFSQEVFPYFNPMKCPVPMTLC 200
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 7-78 5.99e-44

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


:

Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 149.13  E-value: 5.99e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903   7 VNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 93-132 1.46e-22

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


:

Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 90.25  E-value: 1.46e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTE 132
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLLE 40
TMF_TATA_bd super family cl26375
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 130-175 6.00e-06

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


The actual alignment was detected with superfamily member pfam12325:

Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 45.23  E-value: 6.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530395903  130 LTEEVArEYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQ 175
Cdd:pfam12325  69 LEKELK-ELEQRYETTLELLGEKSEEVEELKADVEDLKEMYREQVQ 113
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-240 5.30e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 130 LTEEVAREYQV-----KLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRdildwEESNELQNLE 204
Cdd:COG1196  283 LEEAQAEEYELlaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----EAEEELEEAE 357

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530395903 205 KEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
 288-489 6.77e-118

PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction.


Pssm-ID: 293994  Cd Length: 200  Bit Score: 344.59  E-value: 6.77e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 288 FRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGargtryqtFVNFNYCTGILGSQSITSGKHYWEVDVSK 367
Cdd:cd15822    1 FNELTDVQRYWVHVTLDPSNNKNIVISEDRRQVRYVRKQQRYN--------SNGNNEDYGVLGSPSITSGKHYWEVDVSK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 368 KTAWILGVCAGFQPDAM---------CNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSvpfIVPLSVIICPDRV 438
Cdd:cd15822   73 KRAWILGVCGGKYPNSTlkdfnkqgkNNQKQCSNYQPKYGYWVIGLQNKSEYNAFEDSSSSDPL---ILTLSLTVPPCRV 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 439 GVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15822  150 GVFLDYEAGTVSFFNVTNHGFLIYKFSSCSFSQEVFPYFNPMKCPVPMTLC 200
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 7-78 5.99e-44

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 149.13  E-value: 5.99e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903   7 VNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 93-132 1.46e-22

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 90.25  E-value: 1.46e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTE 132
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLLE 40
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 356-491 1.69e-19

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 84.27  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   356 SGKHYWEVDVSKKTAWILGVCagfqpdamcniekNENYQPKY--------GYWVIgleEGVKCSAFQDSSFHTPSVPFIV 427
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVA-------------TKSVPRGYfallgedkGSWGY---DGDGGKKYHNSTGPEYGLPLQE 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395903   428 PlsviicPDRVGVFLDYEACTVSFFNITNHgFLIYKFSHCSFSQPVFPYLNPR-KCGVPMTLCSP 491
Cdd:smart00449  65 P------GDVIGCFLDLEAGTISFYKNGKY-LHGLAFFDVKFSGPLYPAFSLGsGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 358-476 6.45e-17

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 76.61  E-value: 6.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  358 KHYWEVDVS--KKTAWILGVC-AGFQpdamcniEKNENYQ-PKYGYWVIGLEEGVKCSAfqdSSFHTPSVPFIVPlsvii 433
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWAtKSVP-------RKGERFLgDESGSWGYDGWTGKKYWA---STSPLTGLPLFEP----- 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530395903  434 cPDRVGVFLDYEACTVSFFNitNHGFLIYKFSHCSFSQPVFPY 476
Cdd:pfam00622  66 -GDVIGCFLDYEAGTISFTK--NGKSLGYAFRDVPFAGPLFPA 105
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 15-56 3.87e-09

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 52.02  E-value: 3.87e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530395903   15 CPICLELLTQPLsLDCGHSFCQACLTANHKKSmldKGESSCP 56
Cdd:pfam13445   1 CPICLELFTDPV-LPCGHTFCRECLEEMSQKK---GGKFKCP 38
BBOX smart00336
B-Box-type zinc finger;
90-130 3.06e-08

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 49.64  E-value: 3.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 530395903    90 QKVDHCARHG-EKLLLFCQEDGKVICWLCERSqEHRGHHTFL 130
Cdd:smart00336   1 QRAPKCDSHGdEPAEFFCEECGALLCRTCDEA-EHRGHTVVL 41
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 15-58 8.68e-08

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 48.27  E-value: 8.68e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530395903    15 CPICLE-LLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVC 58
Cdd:smart00184   1 CPICLEeYLKDPVILPCGHTFCRSCI-----RKWLESGNNTCPIC 40
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 130-175 6.00e-06

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 45.23  E-value: 6.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530395903  130 LTEEVArEYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQ 175
Cdd:pfam12325  69 LEKELK-ELEQRYETTLELLGEKSEEVEELKADVEDLKEMYREQVQ 113
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 15-78 1.16e-05

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 47.69  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903   15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKgESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:TIGR00599  29 CHICKDFFDVPVLTSCSHTFCSLCI-----RRCLSN-QPKCPLCRAEDQESKLRSNWLVSEIVE 86
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-240 5.30e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 130 LTEEVAREYQV-----KLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRdildwEESNELQNLE 204
Cdd:COG1196  283 LEEAQAEEYELlaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----EAEEELEEAE 357

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530395903 205 KEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 142-255 1.35e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.90  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 142 LQAALEMLRQK----QQEAEELEADIREekasWKTQIQYDKTNVLADFEQLRDILDWEES----NELQNLEKEEEDILKS 213
Cdd:cd22656  119 IKALLDDLLKEakkyQDKAAKVVDKLTD----FENQTEKDQTALETLEKALKDLLTDEGGaiarKEIKDLQKELEKLNEE 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903 214 LTNsetEMVQQTQSLRELISDLEH------RLQGSVMELLQGVDGVIK 255
Cdd:cd22656  195 YAA---KLKAKIDELKALIADDEAklaaalRLIADLTAADTDLDNLLA 239
zf-B_box pfam00643
B-box zinc finger;
90-128 1.58e-04

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 38.99  E-value: 1.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530395903   90 QKVDHCARHG-EKLLLFCQEDGKVICWLCERSqEHRGHHT 128
Cdd:pfam00643   1 SKERLCPEHEeEPLTLYCNDCQELLCEECSVG-EHRGHTV 39
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 15-67 1.93e-04

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 43.34  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKgessCPVCRISYQPENI 67
Cdd:COG5574  218 CFLCLEEPEVPSCTPCGHLFCLSCLLISWTKKKYEF----CPLCRAKVYPKKV 266
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-272 1.44e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   127 HTFLTEEVA--REYQVKLQAALEmLRQKQQEAEELEADIREEKAS----------------WKTQIQYDKTNVLADFEQL 188
Cdd:pfam02463  155 RLEIEEEAAgsRLKRKKKEALKK-LIEETENLAELIIDLEELKLQelklkeqakkaleyyqLKEKLELEEEYLLYLDYLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   189 RDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLREL---ISDLEHRLQGSVMELLQgvdgvIKRTENVTLKKP 265
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEE-----ELKSELLKLERR 308


                   ....*..
gi 530395903   266 ETFPKNQ 272
Cdd:pfam02463  309 KVDDEEK 315
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
132-238 1.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 132 EEVAREYQVKLQAALEMLRQKQQEAEELEADIRE----------EKASWKTQIQyDKTNVLADFEQ----LRDILDWEE- 196
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETLEAEIEDlretiaeterEREELAEEVR-DLRERLEELEEerddLLAEAGLDDa 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903 197 -----SNELQNLEKEEEDILKSLTN---SETEMVQQTQSLRELISDLEHR 238
Cdd:PRK02224 308 daeavEARREELEDRDEELRDRLEEcrvAAQAHNEEAESLREDADDLEER 357
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
10-153 2.80e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.00  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQAC---LTANHKKsmldkgeSSCPVCRISYQpENIRPNRHVANIVE----KLRE 82
Cdd:COG5236   59 EENMNCQICAGSTTYSARYPCGHQICHACavrLRALYMQ-------KGCPLCRTETE-AVVFTASSPADITDrrqwKGRE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903  83 VKLSPEGQKVDHCARHGEKLLLFCQEDG-KVICWLCERSQEHRG--HHTFLTEEVAREYQVkLQAALEMLRQKQ 153
Cdd:COG5236  131 EKVGIFYEGEDVRDEMEDLLSFKCPKSKcHRRCGSLKELKKHYKaqHGFVLCSECIGNKKD-FWNEIRLFRSST 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-239 2.96e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   130 LTEEVA--REYQVKLQAALEMLRQKQQEAEELEADIRE----------EKAswkTQIQYDKTNvladfEQLRDILDWEES 197
Cdd:TIGR02169  158 IIDEIAgvAEFDRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrERE---KAERYQALL-----KEKREYEGYELL 229

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 530395903   198 NELQNLEKEEEDILKSLTNSETEMVQqtqsLRELISDLEHRL 239
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEK----LTEEISELEKRL 267
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 6-69 5.89e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 38.14  E-value: 5.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903   6 LVNVKEEVTCPICLELLTQPLSLDCGHSFCQACL-----TANHKKSMLDKGE-----SSCPVCRISYQPENIRP 69
Cdd:PLN03208  12 LVDSGGDFDCNICLDQVRDPVVTLCGHLFCWPCIhkwtyASNNSRQRVDQYDhkrepPKCPVCKSDVSEATLVP 85
 
Name Accession Description Interval E-value
SPRY_PRY_TRIM5 cd15822
PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger ...
 288-489 6.77e-118

PRY/SPRY domain in tripartite motif-binding protein 5 (TRIM5), also known as RING finger protein 88 (RNF88); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM5 which is also known as RING finger protein 88 (RNF88) or TRIM5alpha (TRIM5a), an antiretroviral restriction factor and a retrovirus capsid sensor in immune signaling. TRIM5 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It blocks retrovirus infection soon after the virion core enters the cell cytoplasm by recognizing the capsid protein lattice that encases the viral genomic RNA; the SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. TRIM5a, an E3 ubiquitin ligase, promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, and amplifies these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction.


Pssm-ID: 293994  Cd Length: 200  Bit Score: 344.59  E-value: 6.77e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 288 FRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGargtryqtFVNFNYCTGILGSQSITSGKHYWEVDVSK 367
Cdd:cd15822    1 FNELTDVQRYWVHVTLDPSNNKNIVISEDRRQVRYVRKQQRYN--------SNGNNEDYGVLGSPSITSGKHYWEVDVSK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 368 KTAWILGVCAGFQPDAM---------CNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSvpfIVPLSVIICPDRV 438
Cdd:cd15822   73 KRAWILGVCGGKYPNSTlkdfnkqgkNNQKQCSNYQPKYGYWVIGLQNKSEYNAFEDSSSSDPL---ILTLSLTVPPCRV 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 439 GVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15822  150 GVFLDYEAGTVSFFNVTNHGFLIYKFSSCSFSQEVFPYFNPMKCPVPMTLC 200
SPRY_PRY_TRIM5_6_22_34 cd15810
PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and ...
 300-489 1.86e-104

PRY/SPRY domain of tripartite motif-binding protein 5, 6, 22 and 34 (TRIM5, TRIM6, TRIM22 and TRIM34); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of very close paralogs, TRIM5, TRIM6, TRIM22 and TRIM34. These domains are composed of RING/B-box/coiled-coil core and are also known as RBCC proteins. They form a locus of four closely related TRIM genes within an olfactory receptor-rich region on chromosome 11 of the human genome. Genetic analysis of this locus indicates that these four genes have evolved by gene duplication from a common ancestral gene. All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties. TRIM5 promotes innate immune signaling by activating the TAK1 kinase complex by cooperating with the heterodimeric E2, UBC13/UEV1A. It also stimulates NFkB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines, amplifying these activities upon retroviral infection. Interaction of its PRY-SPRY or cyclophilin domains with the retroviral capsid lattice stimulates the formation of a complementary lattice by TRIM5, with greatly increased TRIM5 E3 activity, and host cell signal transduction. TRIM6 is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response. TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. While the PRY-SPRY domain of TRIM5a provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293982 [Multi-domain]  Cd Length: 189  Bit Score: 309.80  E-value: 1.86e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNIS-CAVISEDKRQVSSPKPQiiygargTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAG 378
Cdd:cd15810    1 DVTLNPVNISlNIVISEDQRQVRIVPPQ-------TSGQALTNNNYDFGVLGSQYFSSGKHYWEVDVSKKSAWILGVCSH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 379 FQPDAMCNI--------EKNENYQPKYGYWVIGLEEGVKCSAFQDSSfhtPSVPFIVPLSVIICPDRVGVFLDYEACTVS 450
Cdd:cd15810   74 KRSDAMTKSnanqinhqNVYSRYQPQYGYWVIGLQNESEYNAFEDSS---SFNPHVLTLSVTVPPHRVGVFLDYEAGTVS 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 530395903 451 FFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15810  151 FFNVTNHGSLIYKFSKCCFSTTVCPYFNPWNCPVPMTLC 189
SPRY_PRY_TRIM22 cd15824
PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger ...
 297-491 8.57e-70

PRY/SPRY domain in tripartite motif-containing protein 22 (TRIM22), also known as RING finger protein 94 (RNF94) or Stimulated trans-acting factor of 50 kDa (STAF50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM22, also known as RING finger protein 94 (RNF94) or STAF50 (Stimulated trans-acting factor of 50 kDa). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM22 is an interferon-induced protein, predominantly expressed in peripheral blood leukocytes, in lymphoid tissue such as spleen and thymus, and in the ovary.TRIM22 plays an integral role in the host innate immune response to viruses; it has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 inhibits influenza A virus (IAV) infection by targeting the viral nucleoprotein for degradation; it represents a novel restriction factor up-regulated upon IAV infection that curtails its replicative capacity in epithelial cells. Altered TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. A large number of high-risk non-synonymous (ns)SNPs have been identified in the highly polymorphic TRIM22 gene, most of which are located in the SPRY domain and could possibly alter critical regions of the SPRY structural and functional residues, including several sites that undergo post-translational modification. TRIM22 is a direct p53 target gene and inhibits the clonogenic growth of leukemic cells. Its expression in Wilms tumors is negatively associated with disease relapse. It is greatly under-expressed in breast cancer cells as compared to non-malignant cell lines; p53 dysfunction may be one of the mechanisms for its down-regulation.


Pssm-ID: 293996 [Multi-domain]  Cd Length: 198  Bit Score: 221.26  E-value: 8.57e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 297 YWVDVTVAP-NNISCAVISEDKRQVSSPKPQiiygargtryqTFVNFNYCT----GILGSQSITSGKHYWEVDVSKKTAW 371
Cdd:cd15824    1 YWVDVMLNPvNAVSNVVVSADQRQVTVVHIC-----------MFRNSNPCDfsafDVLGCQYFSSGKYYWEVDVSGKIAW 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 372 ILGVCA-----------GFQPDAMCNIEK-NENYQPKYGYWVIGLEEGVKCSAFQDSSfhtPSVPFIVPLSVIICPDRVG 439
Cdd:cd15824   70 ILGVYSkrnnlnkrkssGFAFDPNVNHPNvYSRYRPQNGYWVIGLQNESEYNAFEDSS---SSDPKVLTLSMAVPPHRVG 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903 440 VFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSP 491
Cdd:cd15824  147 VFLDYEAGTVSFFNVTNHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCPP 198
SPRY_PRY_TRIM34 cd15825
PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger ...
 298-489 2.22e-69

PRY/SPRY domain in tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM34, also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein (IFP1). TRIM34 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. The TRIM21 cDNA possesses at least three kinds of isoforms, due to alternative splicing, of which only the long and medium forms contain the SPRY domain. It is an interferon-induced protein, predominantly expressed in the testis, kidney, and ovary. The SPRY domain provides the capsid recognition motif that dictates specificity to retroviral restriction. While the PRY-SPRY domain provides specificity and the capsid recognition motif to retroviral restriction, TRIM34 binds HIV-1 capsid but does not restrict HIV-1 infection.


Pssm-ID: 293997  Cd Length: 185  Bit Score: 219.71  E-value: 2.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 298 WVDVTVAPNNISC-AVISEDKRQVSSpkpqiiygargTRYQTFVNFNYctGILGSQSITSGKHYWEVDVSKKTAWILGVC 376
Cdd:cd15825    1 WVDFTLNPVNLNLnLVLSEDQRQVTS-----------VPIWPFKCYNY--GILGSQYFSSGKHYWEVDVSKKTAWILGVY 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 377 AGFQPDAMCNIEKNEN-------YQPKYGYWVIGLEEGVKCSAFQDSSfhtPSVPFIVPLSVIICPDRVGVFLDYEACTV 449
Cdd:cd15825   68 CRKRSRTFKYVRQGKNhpnvysrYRPQYGYWVIGLQNKSEYYAFEDSS---TSDPKVLTLSVATPPHRVGVFLDYEAGTV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530395903 450 SFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15825  145 SFFNVTNHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLC 184
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 300-489 1.41e-55

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293968 [Multi-domain]  Cd Length: 174  Bit Score: 183.45  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNISC-AVISEDKRQVSSPKPQIIYGARGTRyqtfvnFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAG 378
Cdd:cd13733    1 DVTLDPDTAHPnLILSEDLKSVRYGDKRQNLPDNPER------FDTCVCVLGSEGFSSGRHYWEVEVGGKTDWDLGVARE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 379 FQpdamcNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSfhtpsvpfiVPLSVIICPDRVGVFLDYEACTVSFFNITNhG 458
Cdd:cd13733   75 SV-----NRKGKITLSPENGYWTVGLRNGNEYKALTSPS---------TPLSLREKPQKVGVFLDYEEGQVSFYNVDD-G 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530395903 459 FLIYKFSHCsFSQPVFPYLNPR-----KCGVPMTLC 489
Cdd:cd13733  140 SHIYTFTDC-FTEKLYPYFSPClndggKNSAPLIIC 174
SPRY_PRY_TRIM6 cd15823
PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger ...
 297-491 2.59e-54

PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM6, also known as RING finger protein 89 (RNF89). TRIM6 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is selectively expressed in embryonic stem (ES) cells and interacts with the proto-oncogene product Myc, maintaining the pluripotency of the ES cells. TRIM6, together with E2 Ubiquitin conjugase (UbE2K) and K48-linked poly-Ub chains, is critical for the IkappaB kinase epsilon (IKKepsilon) branch of type I interferon (IFN-I) signaling pathway and subsequent establishment of a protective antiviral response.


Pssm-ID: 293995  Cd Length: 188  Bit Score: 180.44  E-value: 2.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 297 YWVDVTVAPNNISC-AVISEDKRQVSspkpqiiYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGV 375
Cdd:cd15823    1 YWVDVTLNPHTANLnLVLSKNRRQVR-------FVGAKLSGPSYLEEHYDCSVLGSQHFSSGKHYWEVDVTKKTAWILGV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 376 CA-------GFQPdAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSfhtPSVPfivpLSVIICPDRVGVFLDYEACT 448
Cdd:cd15823   74 CShslgptfSFNQ-YAQNHNAYSRYQPQSGYWVIGLQHNHEYRAYEDSS---TSLL----LSMTVPPRRVGVFLDYEAGT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530395903 449 VSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSP 491
Cdd:cd15823  146 VSFYNVTNHGFPIYTFSKYYFPTTLCPYFNPCNCVVPMTLRRP 188
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 7-78 5.99e-44

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 149.13  E-value: 5.99e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903   7 VNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:cd16591    1 VNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESVNQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 291-489 1.68e-36

PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 133.34  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 291 LTDVRRYWVDVTVAPNNI-SCAVISEDKRQVSspkpqiiYGARGTRY-QTFVNFNYCTGILGSQSITSGKHYWEVDVSKK 368
Cdd:cd15813    1 LRAAQAHAVNVTLDPETAhPNLIFSDDLKSVR-------LGNKWDRLpDNPERFDSCIIVLGSPSFTSGRHYWEVEVGDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 369 TAWILGVCagfqpDAMCNIEKNENYQPKYGYWVIGLeegVKCSAFQDSSFhTPSvpfivPLSVIICPDRVGVFLDYEACT 448
Cdd:cd15813   74 TGWILGVC-----KASVSRKGSMTLSPENGYWVVMM---TKRNEYQASTS-PPT-----RLWLREPPRRVGIFLDYEAGD 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903 449 VSFFNITNHGfLIYKFSHCSFSQPVFPYLNPR-----KCGVPMTLC 489
Cdd:cd15813  140 ISFYNVTAKS-HIYTFTSFSSSGPLQPIFSPGthdggKNMDPLTIC 184
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 297-489 1.29e-34

PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity.


Pssm-ID: 293957  Cd Length: 180  Bit Score: 128.08  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 297 YWVDVTVAPNNI-SCAVISEDKRQVS-SPKPQIIYGARgtryQTFVNFNYctgILGSQSITSGKHYWEVDVSKKTAWILG 374
Cdd:cd12900    1 HMVHITLDPDTAnPWLILSKDRRQVRlGDTHQNVPENE----ERFDNYPM---VLGAQRFNSGKHYWEVDVTGKEAWDLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 375 VCAGfqpdamcNIEKNENY--QPKYGYWVIGLEEGvkcsafqdsSFHTPSVPfIVPLSVIICPDRVGVFLDYEACTVSFF 452
Cdd:cd12900   74 VCRD-------SVRRKGQFllSPENGFWTIWLWNK---------KYEAGTSP-QTTLHLQVPPCQVGIFLDYEAGVVSFY 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530395903 453 NITNHGFLIYKFSHCSFSQPVFPYLNP-----RKCGVPMTLC 489
Cdd:cd12900  137 NITDHGSLIYTFSECAFTGPLRPFFNPgfndsGGNAAPLTLC 178
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 299-490 3.71e-34

PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.


Pssm-ID: 293979 [Multi-domain]  Cd Length: 177  Bit Score: 126.59  E-value: 3.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 299 VDVTVAPN----NIscaVISEDKRQVSspkpqiiygaRGTRYQTFVN----FNYCTGILGSQSITSGKHYWEVDVSKKTA 370
Cdd:cd13745    3 VDVTLDPDtahpNL---VLSEDRKSVR----------HGDTRQDLPDnperFDTYPCVLGAEGFTGGRHYWEVEVGDKTE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 371 WILGVCAgfqpDAMCNIEKNEnYQPKYGYWVIGLEEGvKCSAfqdssfhTPSvPFIvPLSVIICPDRVGVFLDYEACTVS 450
Cdd:cd13745   70 WTLGVCR----ESVSRKGEVT-LSPENGYWTVWLRDG-KYEA-------LTS-PPT-PLPVSVRPSRVGIFLDYEAGEVS 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 530395903 451 FFNITNHGFLiYKFSHcSFSQPVFPYLNP-----RKCGVPMTLCS 490
Cdd:cd13745  135 FYNVTDRSHL-FTFTD-TFSGTLRPYFYPglnagGKNAAPLIICP 177
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 296-489 2.11e-31

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 118.95  E-value: 2.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 296 RYWVDVTVAP---NNisCAVISEDKRQV-SSPKPQiiygargTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAW 371
Cdd:cd15821    1 KFQVDMTLDVdtaNN--YLIISEDLRSVrCGCFRQ-------NRKELAERFDDALCVLGSPRFTSGRHYWEVDVGTSTEW 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 372 ILGVCAgfqpdAMCNIEKNENYQPKYGYWVIGLEEGvkcsafqdSSFHTPSVPFIvPLSVIICPDRVGVFLDYEACTVSF 451
Cdd:cd15821   72 DLGVCR-----ESVNRQGPIELSPEHGFWTVSLRDG--------SVFFASTVPLT-VLWVNPRLHRVGIFLDMEMGTISF 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530395903 452 FNITNhGFLIYKFSHCSFSQPVFPYLNPRKC----GVPMTLC 489
Cdd:cd15821  138 YDVSD-GSHIFTFTKISAEEPLRPFFAPANPygddQGVLSIC 178
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 299-489 1.36e-29

butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells.


Pssm-ID: 293991 [Multi-domain]  Cd Length: 172  Bit Score: 113.86  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 299 VDVTVAPNNISCAVI-SEDKRQVS-SPKPQIIYGARgtryQTFvNFNYCtgILGSQSITSGKHYWEVDVSKKTAWILGVC 376
Cdd:cd15819    2 VNVTLDPDTAHPALIlSEDGRSVTwGETRQDLPENP----ERF-DSLPC--VLGQEGFTSGRHYWEVEVGDRTSWDLGVC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 377 AGfqpdamcNIEKNENYQ--PKYGYWVIGLEEGvKCSAFqdSSFHTpsvpfivPLSVIICPDRVGVFLDYEACTVSFFNI 454
Cdd:cd15819   75 RD-------NVMRKGRVTlsPENGFWAIRLYGN-EYWAL--TSPET-------PLTLKEPPRRVGIFLDYEAGDVSFYNM 137

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530395903 455 TNhGFLIYKFSHCSFSQPVFPYLNPRKCG-VPMTLC 489
Cdd:cd15819  138 TD-GSHIYTFPQTAFSGPLRPFFRLWSSDsGPLTIC 172
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 313-475 3.14e-28

PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg.


Pssm-ID: 293992 [Multi-domain]  Cd Length: 176  Bit Score: 110.21  E-value: 3.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 313 ISEDKR--QVSSPKPQIIYGARgtRYQTFvnfnYCtgILGSQSITSGKHYWEVDVSKKTAWILGVCAGfqpdamcNIEKN 390
Cdd:cd15820   19 ISEDQRslQWADEPQNLPDNPK--RFDWH----YC--VLGCKSFTSGRHFWEVEVGDRKEWYVGVCRE-------NVERK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 391 ENYQ--PKYGYWVIGLEEGVKCSAFQDSSFHtpsvpfivpLSVIICPDRVGVFLDYEACTVSFFNITNhGFLIYKFSHCS 468
Cdd:cd15820   84 LWVKmaPENGFWTIGLSDGNDYQALTDPRTK---------LTIANPPQRVGVFLDYETGEVSFYNAMD-GSHIYTFPHTS 153


                 ....*..
gi 530395903 469 FSQPVFP 475
Cdd:cd15820  154 FSGPLYP 160
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 301-489 1.35e-27

PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism.


Pssm-ID: 293950 [Multi-domain]  Cd Length: 171  Bit Score: 108.49  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 301 VTVAPNNI-SCAVISEDKRQVSspkpqiiygaRGTRYQTFVN----FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGV 375
Cdd:cd12893    2 VTLDPNTAhPWLSLSEDLTSVR----------YSSEKQQLPDnperFDPYPCVLGSEGFTSGKHSWDVEVGDNTSWMLGV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 376 CagfqpdAMCNIEKNENYQ-PKYGYWVIGLEEGvKCSAFqdssfhTPSVPfIVPLSVIICPDRVGVFLDYEACTVSFFNI 454
Cdd:cd12893   72 A------KESVQRKGKFTLsPESGFWTIGFSEG-KYSAR------TSPEP-RTPLRVKQKPQRIRVQLDWDRGKVSFSDP 137

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530395903 455 TNHGfLIYKFSHcSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd12893  138 DTNT-HIHTFTH-TFTERVFPYFYTGCKSEPLRIL 170
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 300-489 3.96e-27

PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293934 [Multi-domain]  Cd Length: 168  Bit Score: 107.01  E-value: 3.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNIScavISEDKRQVSSPKPQIIYGARGTRyqtfvnFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGF 379
Cdd:cd12874    4 DPDTAHLNLI---LSDDLRSVRVGDISQHPPEPPPR------FFECWQVLGSQSFSSGRHYWEVDVQDDSSWYVGVTYKS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 380 QP--DAMCNIEKNEnyqpkyGYWVIGLEEGVkcsaFQDSSFHTPSVPFIVPlsviicPDRVGVFLDYEACTVSFFNITNH 457
Cdd:cd12874   75 LPrkGKMSNLGRNN------GSWCLEWRENE----FSAWHNNPETRLPVTP------PRRLGVFLDCDGGSLSFYGVTDG 138

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530395903 458 GFLIYKFsHCSFSQPVFPYLNPRKCGvPMTLC 489
Cdd:cd12874  139 VQLLYTF-KAKFTEPLYPAFWLGEGS-TLSIC 168
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 292-477 4.14e-26

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 104.74  E-value: 4.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 292 TDVRRYWVDVTVAPNNISCAVI-SEDKRQVSSPKPQIIYGARGTRYQTFvnfnYCtgILGSQSITSGKHYWEVDVSKKTA 370
Cdd:cd15815    6 KMLRRHQVSVTLDPDTAHPELTlSKDQRQVTYGRCQENLDASPKRFTVL----PC--VLGCEGFTSGRHYFEVDVGEGTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 371 WILGVCA-GFQPDAmcNIEKnenyQPKYGYWVIGLEEGVKCSAFQdssfhtpSVPfiVPLSVIICPDRVGVFLDYEACTV 449
Cdd:cd15815   80 WDVGVCLeNVQRGF--GMKQ----EPEFGFWTIRLCEEDGYVALT-------SPP--TPLPLREKPLVVGVFLDYEAGLV 144

                        170       180
                 ....*....|....*....|....*...
gi 530395903 450 SFFNITNhGFLIYKFSHCSFSQPVFPYL 477
Cdd:cd15815  145 SFYNMTT-GSHIFTFPKASFSDTLRPYF 171
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 294-476 4.27e-26

PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites.


Pssm-ID: 294000 [Multi-domain]  Cd Length: 180  Bit Score: 104.68  E-value: 4.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 294 VRRYWVDVTVAPNNISCA-VISEDKRQV--SSPKPQIIYGARgtryqtfvNFNYCTGILGSQSITSGKHYWEVDVSKKTA 370
Cdd:cd15828    5 IKRFQVDVTLDPETAHPQlTVSEDRKSVlyGEMKQNVCYNPR--------RFYLCPAVLGSEGFHSGRQYWEVEVGDKPE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 371 WILGVCAGFQPdamcnieKNENYQP--KYGYWVIGLEEGVKCSAFQDSSFHtpsvpfIVPlsvIICPDRVGVFLDYEACT 448
Cdd:cd15828   77 WTLGVCQDCLP-------RNWSNQPsvQDGLWAIGRYSESNYVALGPKKIQ------LLP---KVRPSKIGIFLDYELGE 140

                        170       180
                 ....*....|....*....|....*...
gi 530395903 449 VSFFNItNHGFLIYKFSHCsFSQPVFPY 476
Cdd:cd15828  141 VSFYNM-NDRSLLYTFSDS-FTGTLWPY 166
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 300-489 7.07e-26

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 103.50  E-value: 7.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNISCA-VISEDKRQVSspkpqiiygaRGTRYQTFVN----FNYCTGILGSQSITSGKHYWEVDVSKKTAWILG 374
Cdd:cd15811    1 DVTLDPDTANPElVLSEDRRSVR----------RGDLRQALPDsperFDPGPCVLGRERFTSGRHYWEVEVGDRTSWALG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 375 VCAGfqpdamcNIEKNENYQ--PKYGYWVIgleegvkcsAFQDSSFHTPSVPFIvPLSViiCPDRVGVFLDYEACTVSFF 452
Cdd:cd15811   71 VCKE-------NVNRKEKGElsAGNGFWIL---------VFLGNYYSSERRTFA-PLRD--PPRRVGIFLDYEAGHLSFY 131

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530395903 453 NITNhGFLIYKFSHCSFSQPVFPYLNPRKCG-VPMTLC 489
Cdd:cd15811  132 SATD-GSLLFIFPETPFSGTLRPLFSPLSSSpTPMTIC 168
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 302-489 1.92e-25

PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 293989 [Multi-domain]  Cd Length: 168  Bit Score: 102.24  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 302 TVAPNNIscavISEDKRQV--SSPKPQIIYGARgtryqtfvNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGF 379
Cdd:cd15817    8 TAHPNLI----VSEDRKAVryRRMKPNCPYDPR--------RFTVYPAVLGSEGFDSGRHFWEVEVGGKGEWILGVCKDS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 380 QPDAMcniekNENYQPKYGYWVIGLeegvkcsafQDSSFHTPSvPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGF 459
Cdd:cd15817   76 LPRNA-----QDPPSPLGGCWQIGR---------YMSGYVASG-PKTTQLLPVVKPSRIGIFLDYELGEVSFYNMNDRSH 140

                        170       180       190
                 ....*....|....*....|....*....|
gi 530395903 460 LiYKFSHCsFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15817  141 L-YTFTDT-FTGKLIPYFYVGPDSEPLTIC 168
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 342-479 4.31e-25

PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle.


Pssm-ID: 293990 [Multi-domain]  Cd Length: 187  Bit Score: 101.80  E-value: 4.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVcagfqpdAMCNIEKNENY--QPKYGYWVIGLEEGVKCSAFQDSSFh 419
Cdd:cd15818   51 FDSSVAVLGSEGFTSGKHYWEVEVAKKTKWTLGV-------VRESINRKGNCplSPEDGFWLLRLRNQNELKALDVPSF- 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903 420 tpsvpfivPLSVIICPDRVGVFLDYEACTVSFFNIT--NHgflIYKFShCSFSQPVFPYLNP 479
Cdd:cd15818  123 --------SLTLTSNLNKVGIYLDYEGGQVSFYNANtmSH---IYTFS-DTFTEKIYPYFCP 172
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 312-489 4.22e-24

zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis.


Pssm-ID: 293962 [Multi-domain]  Cd Length: 178  Bit Score: 99.02  E-value: 4.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 312 VISEDKRQVSSPKPQIIYGARGTRYQTFVNfnyctgILGSQSITSGKHYWEVDVSKKTAWILGVcagfqpdAMCNIEKNE 391
Cdd:cd12905   18 ILSRDLTAVTESDEMQPYPRSPKRFLQCVN------VLASQGFQSGRHYWEVWVGSKTKWDLGV-------ASESVDRQA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 392 NYQ--PKYGYWVIGLEEGVKCSAfqdssfhtPSVPFiVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLiykfshCSF 469
Cdd:cd12905   85 RVKlcPENGYWTLRLRNGDEYWA--------GTQPW-TRLRVTSRPQRIGVFLDCEERKVSFYNADDMSLL------YSF 149

                        170       180
                 ....*....|....*....|....*....
gi 530395903 470 SQP----VFPYLNP-----RKCGVPMTLC 489
Cdd:cd12905  150 HQGprgkVFPFFSTcfsddGQNAEPMRLL 178
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 348-476 1.05e-23

PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein.


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 97.55  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 348 ILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPdamcniEKNENYQ-PKYGYWVIGLEEG----VKCSafqdssfhtPS 422
Cdd:cd15816   44 VLGLQSFSSGRHYWEVAVGEKAEWGLGVCQDSAP------RKGETTPsPENGVWAVWLLKGneymVLAS---------PS 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903 423 VPFIVPLSviicPDRVGVFLDYEACTVSFFNITnHGFLIYKFSHcSFSQPVFPY 476
Cdd:cd15816  109 VPLLQLRR----PRRVGVFLDYEAGEISFYNVT-AGSHIYTFRQ-LFSGILRPY 156
Bbox2_TRIM5-like cd19761
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, ...
 93-132 1.46e-22

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34, TRIM38 and similar proteins; The family includes TRIM5, TRIM6, TRIM22, TRIM34, and TRIM38, all of which belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM5, also termed RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also termed RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also termed 50 kDa-stimulated trans-acting factor (Staf-50), or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also termed interferon-responsive finger protein 1, or RING finger protein 21 (RNF21), may function as an antiviral protein that contributes to the defense against retroviral infections. TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta-triggered nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome.


Pssm-ID: 380819 [Multi-domain]  Cd Length: 40  Bit Score: 90.25  E-value: 1.46e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTE 132
Cdd:cd19761    1 DHCEHHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLLE 40
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 299-489 3.77e-22

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 93.60  E-value: 3.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 299 VDVTVAPNNISCAVI-SEDKRQVSSPKPQIIYGARGTRyqtfvnFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCA 377
Cdd:cd15814    2 VDVTLDPDTAYPSLIlSDNLRQVRYSYLQQDLPDNPER------FNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 378 gfqpDAMCNiEKNENYQPKYGYWVIGLEEGVKCSAFQDSsfhTPSVPFIVPLSviicpdRVGVFLDYEACTVSFFNITN- 456
Cdd:cd15814   76 ----DSVCR-KGGVTSAPQNGFWAVSLWYGKEYWALTSP---MTALPLRTPLQ------RVGIFLDYDAGEVSFYNVTEr 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530395903 457 -HGFliyKFSHCSFSQPVFPYLNPR----KCGVPMTLC 489
Cdd:cd15814  142 cHTF---TFSHATFCGPVRPYFSLSysggKSAAPLIIC 176
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 300-475 2.68e-21

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293949 [Multi-domain]  Cd Length: 167  Bit Score: 90.77  E-value: 2.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNIScavISEDKRQVSSPKPQIIYGARGTRYQTfvnfnycTGILGSQSITSGKHYWEVDVSKKTAWILGVCA-- 377
Cdd:cd12891    4 DPNTAHNNLA---LSGDLKTVTCSSENQHYPDSPERFTH-------SQVLSTQSFSSGRHYWEVEVSESGGWSVGVAYps 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 378 ----------GFQPDAMCnIEKNENyqpKYGYWvigleegvkcsaFQDSSFHTPSVpfivplsviiCPDRVGVFLDYEAC 447
Cdd:cd12891   74 ierkgdesriGRNDKSWC-LEWQDK---SFSAW------------HNNEETPLPSV----------SSRRLGVYLDYEAG 127

                        170       180
                 ....*....|....*....|....*...
gi 530395903 448 TVSFFNITNHGFLIYKFsHCSFSQPVFP 475
Cdd:cd12891  128 RLSFYELSDPIRHLHTF-TATFTEPLHP 154
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 312-475 4.69e-21

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 90.03  E-value: 4.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 312 VISEDKRQVSSpkpqIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCnIEKNE 391
Cdd:cd13734   13 RLSNDNLTVEY----DPEGSKDQAAVLPRRFTGSPAVLGDVAISSGRHYWEVSVSRSTSYRVGVAYKSAPRDED-LGKNS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 392 nyqpkyGYWVIGLEEGvKCSAFQDSSFHTPSVPFIvplsviicPDRVGVFLDYEACTVSFFNiTNHGFLIYKFsHCSFSQ 471
Cdd:cd13734   88 ------TSWCLSRDNN-RYTARHDGKVVDLRVTGH--------PARIGVLLDYDNGTLSFYD-AESKQHLYTF-HVDFEG 150


                 ....
gi 530395903 472 PVFP 475
Cdd:cd13734  151 PVCP 154
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 294-489 3.21e-20

PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 294001  Cd Length: 187  Bit Score: 88.11  E-value: 3.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 294 VRRYWVDVTVAPN----NIscaVISEDKRQVS-SPKPQIIYGARGTryqtfvnFNYCTGILGSQSITSGKHYWEVDVSKK 368
Cdd:cd15829   14 IKKFRVDVTLDPEtahpNL---LVSEDKKCVTfTKKKQRVPDSPKR-------FTVNPVVLGFPGFHSGRHFWEVEVGDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 369 TAWILGVCAGFQPdamcnIEKNENYQPKYGYWVIGLeegvkcsafQDSSFHTP-SVPFIVPLSVIicPDRVGVFLDYEAC 447
Cdd:cd15829   84 PEWAVGVCKDSLS-----TKARRPPSGQQGCWRIQL---------QGGDYDAPgAVPPPLLLEVK--PRGIGVFLDYELG 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530395903 448 TVSFFNITN--HgflIYKFSHcSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd15829  148 EISFYNMPEksH---IHTFTD-TFSGPLRPYFYVGPDSKPLRIC 187
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 11-83 6.30e-20

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 83.80  E-value: 6.30e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKksmldKGESSCPVCRISYQPENIRPNRHVANIVEKLREV 83
Cdd:cd16596    8 EEVTCPICLDPFVEPVSIECGHSFCQECISQVGK-----GGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEI 75
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 342-478 1.37e-19

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 86.39  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGfqpdaMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQdssfhTP 421
Cdd:cd13743   50 FDYSNCVLASRGFSSGKHYWEVVVGSKSKWRLGLIKG-----TTSRKGKLNKSPENGVWLIGLKEGRVYEAFA-----NP 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 422 SVPfiVPLSVIicPDRVGVFLDYEACTVSFFNITNHGFL--IYKFsHCSFSQPVFPYLN 478
Cdd:cd13743  120 RVP--LPLSTR--PQRIGVFLDYEKGELTFYNADSPDELvpIYTF-QAEFQGKLYPLLD 173
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 356-491 1.69e-19

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 84.27  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   356 SGKHYWEVDVSKKTAWILGVCagfqpdamcniekNENYQPKY--------GYWVIgleEGVKCSAFQDSSFHTPSVPFIV 427
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVA-------------TKSVPRGYfallgedkGSWGY---DGDGGKKYHNSTGPEYGLPLQE 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395903   428 PlsviicPDRVGVFLDYEACTVSFFNITNHgFLIYKFSHCSFSQPVFPYLNPR-KCGVPMTLCSP 491
Cdd:smart00449  65 P------GDVIGCFLDLEAGTISFYKNGKY-LHGLAFFDVKFSGPLYPAFSLGsGNSVRLNFGPL 122
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 312-477 2.33e-19

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 85.30  E-value: 2.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 312 VISEDKRQVSspkpqiiygaRGTRYQTFVN----FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVcagfqpdAMCNI 387
Cdd:cd12888   14 VLSEDRKSVR----------WGDTRQDLPDnperFDTWPCVLGCEGFTSGRHYWEVEVGDGGGWAVGV-------ARESV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 388 EKNE--NYQPKYGYWVIGLEEGvKCSAFqdSSFHTPsvpfiVPLSviICPDRVGVFLDYEACTVSFFNiTNHGFLIYKFS 465
Cdd:cd12888   77 RRKGeiSFSPEEGIWAVGQWGG-QYWAL--TSPETP-----LPLS--EVPRRIRVYLDYEGGQVAFFD-ADNEAPIFTFP 145

                        170
                 ....*....|...
gi 530395903 466 HCSFS-QPVFPYL 477
Cdd:cd12888  146 PASFAgERIFPWF 158
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 342-478 4.43e-19

PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23.


Pssm-ID: 293954  Cd Length: 191  Bit Score: 84.97  E-value: 4.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDamcniEKNENYQPKYGYWVIGLEEGVKCSAFQDssfhtP 421
Cdd:cd12897   50 FDKSTCVVASQGFSEGEHYWEVVVGDKPRWALGVIKGTASR-----KGKLHASPSHGVWLIGLKEGKVYEAHGE-----P 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 422 SVPfiVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFL--IYKFsHCSFSQPVFPYLN 478
Cdd:cd12897  120 KEP--RPLRVAGRPHRIGVYLSFEDGVLSFFDASDPDDLrtLYTF-QERFQGKLYPFFD 175
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 9-71 1.73e-17

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 76.36  E-value: 1.73e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMlDKGESSCPVCRISYQPENIRPNR 71
Cdd:cd16598    1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSCITDYCPISG-GHERPVCPLCRKPFKKENIRPNW 62
SPRY_PRY_TRIM17 cd15812
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING ...
 349-483 2.48e-17

PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (terf). TRIM17 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein, expressed almost exclusively in the testis. It exhibits E3 ligase activity, causing protein degradation of ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates proliferation of breast cancer cells. TRIM17 undergoes ubiquitination in COS7 fibroblast-like cells but is inhibited and stabilized by TRIM44.


Pssm-ID: 293984 [Multi-domain]  Cd Length: 176  Bit Score: 79.54  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 349 LGSQSITSGKHYWEV--DVSKKTAWILGVCAGfqpdamcNIEKNENY--QPKYGYWVIGLEEGVKcsafqdssfHTPSVP 424
Cdd:cd15812   45 VGQETFSSGRHYWEVgmNLTGDALWALGVCRD-------NVSRKDRVpkSPENGFWVVQLSKGKK---------YLSAMS 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395903 425 FIVPLSVIICPDRVGVFLDYEACTVSFFNITNhGFLIYKFSHCSFSQPVFPY--LNPRKCG 483
Cdd:cd15812  109 ALTPVTLTEPPSHMGIFLDFEAGEVSFYSVND-GSHLHTYSQAAFPGPLQPFfcLGAPKSG 168
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 358-476 6.45e-17

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 76.61  E-value: 6.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  358 KHYWEVDVS--KKTAWILGVC-AGFQpdamcniEKNENYQ-PKYGYWVIGLEEGVKCSAfqdSSFHTPSVPFIVPlsvii 433
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWAtKSVP-------RKGERFLgDESGSWGYDGWTGKKYWA---STSPLTGLPLFEP----- 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530395903  434 cPDRVGVFLDYEACTVSFFNitNHGFLIYKFSHCSFSQPVFPY 476
Cdd:pfam00622  66 -GDVIGCFLDYEAGTISFTK--NGKSLGYAFRDVPFAGPLFPA 105
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 8-71 6.49e-17

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 74.65  E-value: 6.49e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903   8 NVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVCRISYQPENIRPNR 71
Cdd:cd16594    1 SLQEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEP---ETSASCPQCRETCPQRNLRPNR 61
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 15-83 2.25e-15

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 71.56  E-value: 2.25e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVCRISYQPENIRPNRHVANIVEKLREV 83
Cdd:cd16498   19 CPICLELLKEPVSTKCDHQFCRFCILKLLQKK---KKPAPCPLCKKSVTKRSLQESTRFKQLVEAVKKL 84
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 10-79 1.30e-14

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 68.49  E-value: 1.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKsmLDKGESSCPVCRISYQ--PEnIRPNRHVANIVEK 79
Cdd:cd16597    3 EEELTCSICLELFKDPVTLPCGHNFCGVCIEKTWDS--QHGSEYSCPQCRATFPrrPE-LHKNTVLRNIVEQ 71
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 273-479 4.63e-14

PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage.


Pssm-ID: 293976 [Multi-domain]  Cd Length: 192  Bit Score: 70.66  E-value: 4.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 273 RRVFRApdlkgMLEVFRELT---DVRRYWVDVTVAPNNISCAvisEDKRQVSSPKPQiiygargtryqtfvNFNYCTGIL 349
Cdd:cd13742    1 RKMFRA-----LMPALENLTfdpDTAHPYLVVSSDGKRVECA---DQKQAVSSDDPN--------------RFDKANCVV 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 350 GSQSITSGKHYWEVDVSKKTAWILGVCAgfqpdAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSfhTPSVpfivpL 429
Cdd:cd13742   59 SHQSFSEGEHYWEVIVGDKPRWALGVIS-----AEAGRKGRLHALPSNGFWLLGCKEGKVYEAHVEHK--EPRA-----L 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 430 SVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFS-HCSFSQPVFPYLNP 479
Cdd:cd13742  127 RVEGRPTRIGVYLSFSDGVLSFYDASDEDNLVQLFAfHERFPGPLYPFFDV 177
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
 8-71 6.17e-14

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438257 [Multi-domain]  Cd Length: 70  Bit Score: 66.55  E-value: 6.17e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   8 NVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESS------CPVCRISYQPENIRPNR 71
Cdd:cd16595    1 RLQEEATCSICLDYFTDPVMTTCGHNFCRACIQLSWEKARGKKGRRKqkgsfpCPECREMSPQRNLRPNR 70
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
 8-70 6.81e-14

RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.


Pssm-ID: 438252 [Multi-domain]  Cd Length: 61  Bit Score: 66.21  E-value: 6.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395903   8 NVKEEVTCPICLELLTQPLSLDCGHSFCQACLtanHKKSMLDKGESSCPVCRISYQPENIRPN 70
Cdd:cd16590    2 DIQEELTCPICLDYFQDPVSIECGHNFCRGCL---HRNWAPGGGPFPCPECRHPSAPAALRPN 61
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 9-78 1.23e-13

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 65.56  E-value: 1.23e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:cd16599    1 FKEELLCPICYEPFREAVTLRCGHNFCKGCV----SRSWERQPRAPCPVCKEASSSDDLRTNHTLNNLVE 66
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
 11-59 1.93e-13

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 64.85  E-value: 1.93e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTaNHKKSMLDKGESSCPVCR 59
Cdd:cd16583    4 EEGVCPICQEPLKEAVSTDCGHLFCRMCLT-QHAKKASASGVFSCPVCR 51
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 342-479 2.34e-13

PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML.


Pssm-ID: 293978  Cd Length: 188  Bit Score: 68.49  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCagfqpDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDssfhtp 421
Cdd:cd13744   51 FDVEVSVLGSEGFSGGVHYWEVVVSEKTQWMIGLA-----HEAVSRKGSIQIQPGRGFYCIVMHDGNQYSACTE------ 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530395903 422 svPFiVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLiYKFSHcSFSQPVFPYLNP 479
Cdd:cd13744  120 --PW-TRLNVKSKLEKVGVYLDYDKGLLIFYNADDMSWL-YTFRE-KFPGKLCSYFSP 172
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 301-488 2.37e-13

PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration.


Pssm-ID: 293998 [Multi-domain]  Cd Length: 170  Bit Score: 67.97  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 301 VTVAPNNISCA-VISEDKRQVsspkpqiiygaRGTR-YQTF----VNFNYCTGILGSQSITSGKHYWEVDVSKKTawiLG 374
Cdd:cd15826    2 VTLDPQTASGSlVLSEDRKSV-----------RYTRqKQNLpdspLRFDGLPAVLGSPGFSSGRHRWQVEVQLGD---GG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 375 VCA-GFQPDAMcnieknenyqPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFI-VPLSVIicPDRVGVFLDYEACTVSFF 452
Cdd:cd15826   68 GCTvGVAGESV----------RRKGEMGLSAEDGVWAVILSHQQCWASTSPGTdLPLSEI--PRRVGVALDYEAGTVTLT 135

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530395903 453 NITNHGfLIYKFShCSFSQPVFPYLNPRKCGVPMTL 488
Cdd:cd15826  136 NAETQE-PIFTFT-ASFSGKVFPFFAVWKKGSRLTL 169
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 11-70 6.59e-13

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438274 [Multi-domain]  Cd Length: 60  Bit Score: 63.22  E-value: 6.59e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmlDKGESSCPVCRISYQPENIRPN 70
Cdd:cd16612    3 QDLSCPLCLKLFQSPVTTECGHTFCQDCLSRVPKEE--DGGSTSCPTCQAPTKPEQLSIN 60
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 302-475 8.09e-13

PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25.


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 66.38  E-value: 8.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 302 TVAPNNISCAV-ISEDKRQVSSPKPQIIYGARGTRYQTfvnfnycTGILGSQSITSGKHYWEVDVSKKTAWILGVcagfq 380
Cdd:cd12902    2 TFDLRSLSCSLeVSEDSRKVTVSHGPQAYAWSPDRFSI-------SQVLCSQAFSSGQHYWEVDTRQCSHWAVGV----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 381 pdAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSfhtpsvpfivplSVII---CPDRVGVFLDYEACTVSFFNITNH 457
Cdd:cd12902   70 --ASWEMSRDQMLGRTMDSWCIEWKGTGQLSAWHMNK------------ETVLgsdKPRVVGIWLDLEEGKLAFYSVANQ 135

                        170
                 ....*....|....*...
gi 530395903 458 GFLIYKFShCSFSQPVFP 475
Cdd:cd12902  136 ERLLHECE-VSASSPLHP 152
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
 8-66 2.75e-12

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 61.85  E-value: 2.75e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   8 NVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGES-SCPVCRISYQPEN 66
Cdd:cd16593    1 SLADEVNCPICQGTLREPVTIDCGHNFCRACLTRYCEIPGPDLEEPpTCPLCKEPFRPGE 60
RING-HC_TRIM38_C-IV cd16600
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar ...
 9-59 3.16e-12

RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins; TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438262 [Multi-domain]  Cd Length: 58  Bit Score: 61.33  E-value: 3.16e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLTA---NHKKSMLDKGESSCPVCR 59
Cdd:cd16600    2 MREEATCSICLQLMTEPVSINCGHSYCKRCIVSfleNQSQLEPGLETFSCPQCR 55
Bbox2_TRIM68_C-IV cd19795
B-box-type 2 zinc finger found in tripartite motif-containing protein 68 (TRIM68) and similar ...
 93-135 3.62e-12

B-box-type 2 zinc finger found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380853 [Multi-domain]  Cd Length: 44  Bit Score: 60.92  E-value: 3.62e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVA 135
Cdd:cd19795    2 DLCERHKEKLNLFCEEDQELLCVVCEQSPEHKAHTVVPVEEAA 44
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 11-70 6.10e-12

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 60.54  E-value: 6.10e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVCRISYQPENIRPN 70
Cdd:cd16611    3 EELHCPLCLDFFRDPVMLSCGHNFCQSCITGFWELQ---AEDTTCPECRELCQYRNLTPN 59
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 342-479 1.01e-11

PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells.


Pssm-ID: 293981  Cd Length: 191  Bit Score: 63.70  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCagfQPDAMcNIEKNENYQPKYGYWVIGleegvkcsaFQDSSFHTP 421
Cdd:cd15809   60 FQHLPCVLGKNVFTSGKHYWEVENRDSLEIAVGVC---REDVM-GITDGSEMSPHVGIWAIC---------WSSAGYRPL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 422 SVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNhGFLIYKFShCSFSQPVFPY--LNP 479
Cdd:cd15809  127 TSSPVSPTKQEPALHRVGVFLDHGAGEVSFYSAVD-GVHLHTFS-CPLVSRLRPFfwLSP 184
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 11-69 1.23e-11

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 59.69  E-value: 1.23e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMldKGESSCPVCRisyQPENIRP 69
Cdd:cd16609    2 EELTCSICLGLYQDPVTLPCQHSFCRACIEDHWRQKD--EGSFSCPECR---APFPEGP 55
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 300-490 1.70e-11

PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 240499 [Multi-domain]  Cd Length: 199  Bit Score: 63.24  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 300 DVTVAPNNISCAV-ISEDKRQVSspkpqiiygaRGTRYQTFVNF------NYCtgILGSQSITSGKHYWEVDVSKKTAWI 372
Cdd:cd13741    1 DLTLDPDTAHPALlLSPDRRGVR----------LAERRQEVPEHpkrfsaDCC--VLGAQGFRSGRHYWEVEVGGRRGWA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 373 LGVC------------AGFQPDAMCNIEKNENYQPKYGYWVIG--LEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRV 438
Cdd:cd13741   69 VGAAresthhkekvgsGGSSVSSGDASSSRHHHRRRRLHLPQQplLQREVWCVGTNGKRYQAQSSTEQTLLSPSEKPRRF 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903 439 GVFLDYEACTVSFFNITNHGFlIYKFSHCSFSQPVFPYLNPRKCGVPMTLCS 490
Cdd:cd13741  149 GVYLDYEAGRLGFYNAETLAH-VHTFSAAFLGERVFPFFRVLSKGTRIKLCP 199
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
 12-68 3.37e-11

RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) and similar proteins; AtBRCA1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBRCA1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438509 [Multi-domain]  Cd Length: 54  Bit Score: 58.25  E-value: 3.37e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMldKGESSCPVCRISYQPENIR 68
Cdd:cd23147    4 ELKCPICLSLFKSAANLSCNHCFCAGCI----GESL--KLSAICPVCKIPATRRDTR 54
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 313-475 4.59e-11

SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation.


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 61.28  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 313 ISEDKRQV--SSPKPQIIYGARGTRYQTFVNfnyctgILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPdamcniEKN 390
Cdd:cd12904   14 LSEDRRTLtfSPKKARQSPPDDPERFDHWPN------ALASLSFSSGTHAWVVDVGKSCAYKVGVCYGSLE------RKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 391 ENYQPKYGY----WVIGLEEGvkcsafqDSSFHTPSVPfiVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLiykFSH 466
Cdd:cd12904   82 SGNEARLGYnafsWVFSRYDG-------EFSFSHNGQH--VPLELLKCPARVGVLLDWPSQELLFYDPDSCTVL---HSH 149

                        170
                 ....*....|
gi 530395903 467 -CSFSQPVFP 475
Cdd:cd12904  150 rEAFAAPLLP 159
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
 15-59 5.04e-11

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.


Pssm-ID: 438266 [Multi-domain]  Cd Length: 49  Bit Score: 57.82  E-value: 5.04e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSmlDKGESSCPVCR 59
Cdd:cd16604    3 CPICLDLLKDPVTLPCGHSFCMGCLGALWGAG--RGGRASCPLCR 45
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 10-70 5.94e-11

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 57.63  E-value: 5.94e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTanhkksmlDKGESSCPVCRISYQPENIRPN 70
Cdd:cd16602    1 QEEAVCAICLDYFKDPVSIGCGHNFCRVCVT--------QLWGFTCPQCRKSFPRRSFRPN 53
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 342-479 9.49e-11

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is similar to the distinct PRY/SPRY subdomain found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking.


Pssm-ID: 293956 [Multi-domain]  Cd Length: 176  Bit Score: 60.57  E-value: 9.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVcagfqpdAMCNIEKNENYQPKYGYWVigLEEGVKCSAFQDSSFH-- 419
Cdd:cd12899   41 FTRCVAVMGSLIPVRGKHYWEVEVDEQTEYRVGV-------AFEDTQRNGYLGANNTSWC--MRHIITPSRHKYEFLHng 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903 420 -TPSVPFIVPlsviicPDRVGVFLDYEACTVSFFN--ITNHGFLI-YKFSHcsFSQPVFPYLNP 479
Cdd:cd12899  112 wTPDIRITVP------PKKIGILLDYDSGRLSFFNvdLAQHLYTFsCQFQH--FVHPCFSLEKP 167
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 348-477 1.85e-10

PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain family contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade.


Pssm-ID: 293973 [Multi-domain]  Cd Length: 173  Bit Score: 59.80  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 348 ILGSQSITSGKHYWEVDVSKKTA-WILGVC------AGFQPDAMCNIEKNENYQPKYG--YWvigleegvkcsAFQDSSF 418
Cdd:cd13738   43 VLSRDSFFSGRHYWEVDLQEAGAgWWVGAAypsigrKGDSEAARLGWNRQSWCLKRYDleYW-----------AFHDGQR 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 419 htpsvpfiVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFsHCSFSQPVFPYL 477
Cdd:cd13738  112 --------SRLRPEDDPDRLGVFLDYEAGILSFYDVTGGMTHLHTF-RATFQEPLYPAL 161
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
 11-59 1.86e-10

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 56.30  E-value: 1.86e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGES---SCPVCR 59
Cdd:cd16592    3 EETTCPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEGNGAegvFCPQCG 54
Bbox2_TRIM21_C-IV cd19772
B-box-type 2 zinc finger found in tripartite motif-containing protein 21 (TRIM21) and similar ...
 93-126 2.28e-10

B-box-type 2 zinc finger found in tripartite motif-containing protein 21 (TRIM21) and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren's syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380830 [Multi-domain]  Cd Length: 40  Bit Score: 55.58  E-value: 2.28e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19772    1 ERCAVHGERLHLFCEEDQKALCLVCAQSQKHRDH 34
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
 11-62 2.59e-10

RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 55.89  E-value: 2.59e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKGESSCPVCRISY 62
Cdd:cd23132    1 EEFLCCICLDLLYKPVVLECGHVFCFWCV----HRCMNGYDESHCPLCRRPY 48
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
 12-59 2.82e-10

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogre's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438272 [Multi-domain]  Cd Length: 49  Bit Score: 55.67  E-value: 2.82e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldkGES-----SCPVCR 59
Cdd:cd16610    1 EVACPICMTFLREPVSIDCGHSFCHSCLSGLWEVP----GESqnwgyTCPLCR 49
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
 11-59 4.44e-10

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438268 [Multi-domain]  Cd Length: 53  Bit Score: 55.25  E-value: 4.44e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGES-SCPVCR 59
Cdd:cd16606    1 EEARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDSAQGGVyACPQCR 50
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 14-58 5.60e-10

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 54.41  E-value: 5.60e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVC 58
Cdd:cd16449    2 ECPICLERLKDPVLLPCGHVFCRECI-----RRLLESGSIKCPIC 41
Bbox2_TRIM7-like cd19762
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM7, TRIM27 and ...
 95-135 7.51e-10

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM7, TRIM27 and similar proteins; The family includes TRIM7 and TRIM27, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM27, also termed RING finger protein 76 (RNF76), or RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. It also inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promotes non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis.


Pssm-ID: 380820 [Multi-domain]  Cd Length: 44  Bit Score: 54.24  E-value: 7.51e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVA 135
Cdd:cd19762    3 CEKHQEPLKLFCKEDKRPICVVCDRSREHRHHTVLPVEEAA 43
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
 11-64 9.15e-10

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438205 [Multi-domain]  Cd Length: 54  Bit Score: 54.32  E-value: 9.15e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKsmlDKGESSCPVCRISYQP 64
Cdd:cd16543    2 DQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDR---KQGVPSCPQCRESFPP 52
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
 12-68 1.12e-09

RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 (AtBARD1) and similar proteins; AtBARD1, also called protein REPRESSOR OF WUSCHEL 1, binds specifically to H3K4me3 regions of target gene (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. It is required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. AtBARD1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438508 [Multi-domain]  Cd Length: 54  Bit Score: 54.01  E-value: 1.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTanhkKSMldKGESSCPVCRISYQPENIR 68
Cdd:cd23146    4 ELKCPICLKLLNRPVLLPCDHIFCSSCIT----DST--KVGSDCPVCKLPYHSQDLR 54
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 342-490 1.42e-09

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 57.27  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVC------AGFQPdamcnieknenYQPKYGYWVIGLEEGvkcsafqd 415
Cdd:cd13740   38 FDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVAresvrrKGLTP-----------FTPEEGVWALQLNGG-------- 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 416 sSFHTPSVPFIVPLSviiCP--DRVGVFLDYEACTVSFFNITN--HgflIYKFsHCSFSQPVFPYLNPRKCGVPMTLCS 490
Cdd:cd13740   99 -QYWAVTSPERTPLS---CGhlSRVRVALDLEVGAVSFYAAEDmrH---IYTF-RVNFQERVFPLFSVCSTGTYLRIWP 169
Bbox2_TRIM39-like cd19780
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM39, TRIM58 and ...
 95-126 2.13e-09

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM39, TRIM58 and similar proteins; The family includes TRIM39 and TRIM58, both of which belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM39, also termed RING finger protein 23 (RNF23), or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability and modulates cell cycle progression and DNA damage responses via stabilization of p21. TRIM39 also negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha (TNFalpha). TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization.


Pssm-ID: 380838 [Multi-domain]  Cd Length: 44  Bit Score: 52.85  E-value: 2.13e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19780    5 CARHREALSLFCEEDQEAVCLVCEISHDHRAH 36
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 313-490 2.29e-09

PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized.


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 56.69  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 313 ISEDKRQVS-SPKPQIIYGARGTRYQTFvnfnyctGILGSQSITSGKHYWEVDVSKKTAwILGVCAGFQP-----DAMCN 386
Cdd:cd12896   25 LSRQNRRAKhGRSAARGVPASPGSFELW-------QVQCTQSFQHGHHYWEVEVSSHSV-TLGVTYPGLPrhkqgGHKDN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 387 IEKNEnyqpkyGYWVIGLEEGvkcsafQDSSFHT------PSVPFivplsviicpDRVGVFLDYEACTVSFFNITNHGFL 460
Cdd:cd12896   97 IGRNP------CSWGLQIQED------SLQAWHNgraqklQGVSY----------RLLGVDLDLEAGTLTFYGLEPGTQR 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530395903 461 IYKFsHCSFSQPVFP--YLNPrkcGVPMTLCS 490
Cdd:cd12896  155 LHTF-HAIFTQPLYPvfWLLE---GRTLTLCH 182
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 313-487 3.64e-09

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies.


Pssm-ID: 293955  Cd Length: 171  Bit Score: 56.09  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 313 ISEDKRQVSSPkpqiiygarGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNEN 392
Cdd:cd12898   17 ISSDRGTVIYF---------HERRRKMSSLTECPSVLGEELPSCGQYYWETTVTRCPAYRLGICSSSASQAGALGEGSTS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 393 yqpkygyWVIgleegvKCSAFQDSS-FHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNiTNHGFLIYKFSHcSFSQ 471
Cdd:cd12898   88 -------WCL------HCVPTSEPCrYTLLHSGIVSDVFVTERPARVGTLLDYNNGRLIFIN-AESGQLLGIFRH-RFAQ 152

                        170
                 ....*....|....*....
gi 530395903 472 PVFPYL---NPRKCGVPMT 487
Cdd:cd12898  153 PCHPAFaleKPGKLELHMG 171
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 15-56 3.87e-09

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 52.02  E-value: 3.87e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530395903   15 CPICLELLTQPLsLDCGHSFCQACLTANHKKSmldKGESSCP 56
Cdd:pfam13445   1 CPICLELFTDPV-LPCGHTFCRECLEEMSQKK---GGKFKCP 38
Bbox2_TRIM16-like cd19769
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, ...
 95-139 4.99e-09

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM16, TRIM29, TRIM47 and similar proteins; This family includes a group of tripartite motif-containing proteins, such as TRIM16, TRIM29 and TRIM47. TRIM16, also termed estrogen-responsive B box protein (EBBP), is a regulator that may play a role in the regulation of keratinocyte differentiation. It may also act as a tumor suppressor through affecting cell proliferation and migration or tumorigenicity in carcinogenesis. TRIM29, also termed ataxia telangiectasia group D-associated protein (ATDC), plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. TRIM16 and TRIM29 belong to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. TRIM47 belongs to the C-IV subclass of TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380827 [Multi-domain]  Cd Length: 46  Bit Score: 51.94  E-value: 4.99e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCeRSQEHRGHHTFLTEEVAREYQ 139
Cdd:cd19769    3 CPIHKKPLELFCRTDQMCICELC-AKEEHRGHDVVTVEEEREKKE 46
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 11-63 6.25e-09

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 51.98  E-value: 6.25e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  11 EEVTCPICLELLTQPLSLD-CGHSFCQACLTanhkkSMLDKGESSCPVCRISYQ 63
Cdd:cd16503    1 ENLTCSICQDLLHDCVSLQpCMHNFCAACYS-----DWMERSNTECPTCRATVQ 49
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
 13-59 7.69e-09

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 51.61  E-value: 7.69e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgesSCPVCR 59
Cdd:cd16550    1 CLCPICLEILVEPVTLPCNHTLCMPCFQSTVEKASL-----CCPLCR 42
RING-HC_TRIM43-like_C-IV cd16603
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
 12-70 8.71e-09

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger.


Pssm-ID: 438265 [Multi-domain]  Cd Length: 59  Bit Score: 51.71  E-value: 8.71e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVCRISYQPENIRPN 70
Cdd:cd16603    4 ELTCPICMNYFIDPVTIDCGHSFCRPCLYLNWQDI---PFLAQCPECRKTTEQRNLKTN 59
Bbox2_TRIM4-like cd19760
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM4, TRIM17, TRIM41, ...
 95-126 1.06e-08

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM4, TRIM17, TRIM41, TRIM52 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM4, TRIM17, TRIM41 and TRIM52. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain. TRIM4, TRIM17 and TRIM41 belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380818 [Multi-domain]  Cd Length: 39  Bit Score: 50.71  E-value: 1.06e-08
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19760    3 CEKHQEPLKLFCEEDEALICVICRESRAHRAH 34
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 348-475 1.19e-08

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.


Pssm-ID: 293960  Cd Length: 169  Bit Score: 54.37  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 348 ILGSQSITSGKHYWEVDVSKKTAWILGVcagfqpdAMCNIEKNEnyqpkygywVIGLEEGVKCSAFQDSSFHTPSVPFIV 427
Cdd:cd12903   46 VLGDTPVTSGRHYWEVTVKRSQEFRIGV-------ADVDMSRDE---------CIGTNESSWVFAYAQRKWYAMVANETV 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903 428 PLSVIICPDRVGVFLDYEACTVSFFNITNhGFLIYKFShCSFSQPVFP 475
Cdd:cd12903  110 PVPLVGKPDRVGLLLDYEAGKLSLVDVEK-NSVVHTMS-AEFRGPVVP 155
RING-HC_TRIM31_C-V cd16582
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar ...
 12-58 1.30e-08

RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins; TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438244 [Multi-domain]  Cd Length: 44  Bit Score: 50.60  E-value: 1.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVC 58
Cdd:cd16582    1 EVICPICLDILQKPVTIDCGHNFCLQCITQIGETS---CGFFKCPLC 44
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 15-61 1.71e-08

second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the second RING-HC finger.


Pssm-ID: 438177 [Multi-domain]  Cd Length: 45  Bit Score: 50.34  E-value: 1.71e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTAnhkksMLDkGESSCPVCRIS 61
Cdd:cd16514    4 CSLCLRLLYEPVTTPCGHTFCRACLER-----CLD-HSPKCPLCRTS 44
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 342-489 1.78e-08

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293971 [Multi-domain]  Cd Length: 169  Bit Score: 53.73  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVigleeGVKCSAFQDSSFHT- 420
Cdd:cd13736   37 FTYCSQVLGLHCFKQGIHYWEVELQKNNFCGVGICYGSMDRQGPESRLGRNSESWCVEWF-----NVKISAWHNNVEKTl 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 421 PSVPfivplsviicPDRVGVFLDYEACTVSFFNITNHGFLIYKFShCSFSQPVFPYLNPRKCGVPMTLC 489
Cdd:cd13736  112 PSTK----------ATRVGVLLNCDHGFVIFFAVQDKVHLMYKFK-VDFTEALYPAFWVFSAGTTLSLC 169
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
 10-69 2.22e-08

RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) and similar propteins; This subfamily includes TRIM43A, TRIM43B and TRIM43C, which are expressed specifically in mouse preimplantation embryos. They contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 50.30  E-value: 2.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVCRisyQPENIRP 69
Cdd:cd23133    1 EETLTCSICQGIFMNPVYLRCGHKFCEACLLLFQEDI---KFPAYCPMCR---QPFNQEY 54
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 15-58 2.36e-08

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 50.05  E-value: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530395903   15 CPICLELLTQPL-SLDCGHSFCQACLtanhkKSMLDKGESSCPVC 58
Cdd:pfam00097   1 CPICLEEPKDPVtLLPCGHLFCSKCI-----RSWLESGNVTCPLC 40
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
 13-59 2.49e-08

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 50.14  E-value: 2.49e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLtanHKKSMLDKGESSCPVCR 59
Cdd:cd16605    1 LLCPICLEVFKEPLMLQCGHSYCKSCL---VSLSGELDGQLLCPVCR 44
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
 15-58 2.56e-08

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 464570 [Multi-domain]  Cd Length: 42  Bit Score: 49.74  E-value: 2.56e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530395903   15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSmlDKGESSCPVC 58
Cdd:pfam15227   1 CPICLDYLEKPVSIECGHSFCLSCINSLQKEP--DGESLLCPQC 42
BBOX smart00336
B-Box-type zinc finger;
90-130 3.06e-08

B-Box-type zinc finger;


Pssm-ID: 197662 [Multi-domain]  Cd Length: 42  Bit Score: 49.64  E-value: 3.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 530395903    90 QKVDHCARHG-EKLLLFCQEDGKVICWLCERSqEHRGHHTFL 130
Cdd:smart00336   1 QRAPKCDSHGdEPAEFFCEECGALLCRTCDEA-EHRGHTVVL 41
Bbox2_TRIM11_C-IV cd19766
B-box-type 2 zinc finger found in tripartite motif-containing protein 11 (TRIM11) and similar ...
 95-135 3.44e-08

B-box-type 2 zinc finger found in tripartite motif-containing protein 11 (TRIM11) and similar proteins; TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM11 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380824 [Multi-domain]  Cd Length: 44  Bit Score: 49.43  E-value: 3.44e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVA 135
Cdd:cd19766    3 CGKHREPLKLFCKDHEALLCVVCERSREHWGHRVVPAEEAA 43
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
 14-62 4.79e-08

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 49.28  E-value: 4.79e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  14 TCPICLELLTQPLSLD-CGHSFCQACLTanhkKSMLDKgeSSCPVCRISY 62
Cdd:cd16506    2 TCPICLDEIQNKKTLEkCKHSFCEDCID----RALQVK--PVCPVCGVVY 45
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
 15-63 5.21e-08

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 438160 [Multi-domain]  Cd Length: 52  Bit Score: 49.43  E-value: 5.21e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSMldkgESSCPVCRISYQ 63
Cdd:cd16497    4 CHCCYDLLVNPTTLNCGHSFCRHCLALWWKSSK----KTECPECRQKWE 48
RING-HC_TRIM60-like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 ...
 12-59 5.94e-08

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 and similar proteins; TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. Both TRIM60 and TRIM75 belong the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B2-box, and two coiled coil domains, as well as a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of the TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 438269 [Multi-domain]  Cd Length: 48  Bit Score: 48.96  E-value: 5.94e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKGES-SCPVCR 59
Cdd:cd16607    1 EASCPICLDYLKDPVTINCGHNFCRSCI----SMSWKDLQDTfPCPVCR 45
Bbox2_TRIM10-like cd19765
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM10, TRIM15, ...
 95-126 6.45e-08

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM10, TRIM15, TRIM26, TRIM31 and similar proteins; This family includes TRIM10, TRIM15, TRIM26 and TRIM31. TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM15, also termed RING finger protein 93 (RNF93), or zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM10, TRIM15 and TRIM26 belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM31 belongs to the C-V subclass of TRIM family of proteins. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380823 [Multi-domain]  Cd Length: 39  Bit Score: 48.62  E-value: 6.45e-08
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19765    3 CEEHGEKIHFFCEDDGKFLCVVCRESREHRTH 34
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 15-77 6.78e-08

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 50.03  E-value: 6.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903  15 CPICLELLTQPLSL-DCGHSFCQACLTanhkksmlDKGESSCPVCRISYQPENIRPNRHVANIV 77
Cdd:cd16496   18 CSRCASILKEPVTLgGCEHVFCRSCVG--------DRLGNGCPVCDTPAWARDLQINRQLDSMV 73
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 347-478 7.20e-08

PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain.


Pssm-ID: 240472  Cd Length: 177  Bit Score: 52.32  E-value: 7.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 347 GILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPdamcnieKNENYQPKYGYWVIgleegVKCSAFQDSSFHTPSVPfI 426
Cdd:cd12892   45 GVAGNVFIDSGRHYWEVVISGSTWYAIGIAYKSAP-------KHEWIGKNSASWVL-----CRCNNNWVVRHNSKEIP-I 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903 427 VPLSVIicpDRVGVFLDYEACTVSFFNITNHGFLiYKFShCSFSQPVFPYLN 478
Cdd:cd12892  112 EPSPHL---RRVGILLDYDNGSLSFYDALNSIHL-YTFD-IAFAQPVCPTFT 158
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 342-475 7.21e-08

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 52.49  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITsGKHYWEVDVSKKTAWIlGVC------AGFQPDAMcnieknenyqpkYGY----WvigleeGVKCS 411
Cdd:cd16040   47 FDYWPQVLCREGLS-GRCYWEVEWSGGGVDI-AVAykgisrKGDGDDSR------------FGYndksW------SLECS 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395903 412 AFQDSSFHTPSVPFI-VPLSviiCPDRVGVFLDYEACTVSFFNITNHGFLIYKFsHCSFSQPVFP 475
Cdd:cd16040  107 PSGYSFWHNNKKTEIsVPSS---SSSRVGVYLDHSAGTLSFYSVSDTMTLLHTV-QTTFTEPLYP 167
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
 10-62 7.62e-08

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 438242 [Multi-domain]  Cd Length: 67  Bit Score: 49.12  E-value: 7.62e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKsmlDKGESSCPVCRISY 62
Cdd:cd16580    9 EEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAK---DAGLVRCPECNQAY 58
Bbox2_TRIM43-like cd19783
B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
 95-141 8.20e-08

B-box-type 2 zinc finger found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64, TRIM77 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, TRIM64C, and TRIM77, whose biological functions remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members (except for TRIM51) belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM51 belongs to unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380841 [Multi-domain]  Cd Length: 53  Bit Score: 48.70  E-value: 8.20e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVK 141
Cdd:cd19783    7 CGTHRETKKLFCEADKSLLCLLCSSSQEHRAHRHYPIEWAAEEHREK 53
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 15-58 8.68e-08

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 48.27  E-value: 8.68e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530395903    15 CPICLE-LLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVC 58
Cdd:smart00184   1 CPICLEeYLKDPVILPCGHTFCRSCI-----RKWLESGNNTCPIC 40
Bbox2_xNF7-like cd19800
B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins; ...
 93-127 9.17e-08

B-box-type 2 zinc finger found in Xenopus laevis nuclear factor 7 (xNF7) and similar proteins; xNF7 is a maternally expressed novel zinc finger nuclear phosphoprotein. It acts as a transcription factor that determines dorsal-ventral body axis. xNF7 harbors a B-box motif that shows high sequence similarity with B-Box-type zinc finger 2 found in tripartite motif-containing proteins (TRIMs). The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380858 [Multi-domain]  Cd Length: 39  Bit Score: 48.16  E-value: 9.17e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHH 127
Cdd:cd19800    1 EVCSEHDEPLKLFCKDDKRLICVICRDSRKHRGHR 35
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
 15-59 1.17e-07

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 438204 [Multi-domain]  Cd Length: 50  Bit Score: 48.34  E-value: 1.17e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16542    4 CAVCLEVLHQPVRTRCGHVFCRPCI-----ATSLRNNTWTCPYCR 43
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
 10-59 1.32e-07

RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.


Pssm-ID: 438418 [Multi-domain]  Cd Length: 56  Bit Score: 48.37  E-value: 1.32e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTA---NHKKSMLDKGESSCPVCR 59
Cdd:cd16762    1 EEDLTCPICCCLFDDPRVLPCSHNFCKKCLEGileGNVRTMLWRPPFKCPTCR 53
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 12-58 1.42e-07

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 47.86  E-value: 1.42e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldKGESSCPVC 58
Cdd:cd16601    1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEEL---DGDFPCPQC 44
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
 13-58 1.60e-07

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 47.62  E-value: 1.60e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKgeSSCPVC 58
Cdd:cd16504    3 FLCPICFDIIKEAFVTKCGHSFCYKCI----VKHLEQK--NRCPKC 42
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 10-59 1.68e-07

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 47.88  E-value: 1.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldkGESSCPVCR 59
Cdd:cd16608    4 KDELLCSICLSIYQDPVSLGCEHYFCRQCITEHWSRS----EHRDCPECR 49
RING-HC_TRY3-like cd23137
RING finger, HC subclass, found in Candida albicans transcriptional regulator of yeast form ...
 11-59 2.08e-07

RING finger, HC subclass, found in Candida albicans transcriptional regulator of yeast form adherence 3 (TRY3) and similar proteins; TRY3 acts as a transcription factor required for yeast cell adherence to silicone substrate. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438499 [Multi-domain]  Cd Length: 53  Bit Score: 47.46  E-value: 2.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMldkgeSSCPVCR 59
Cdd:cd23137    1 DDYACPICMNVAWKPVRLECSHVFCLRCLVKAQKQKK-----DNCPLCR 44
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 11-63 2.62e-07

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 47.40  E-value: 2.62e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  11 EEVTCPICLELLTQPLSL-DCGHSFCQACLTAnhkksMLDKGESSCPVCRISYQ 63
Cdd:cd16544    1 AELTCPVCQEVLKDPVELpPCRHIFCKACILL-----ALRSSGARCPLCRGPVG 49
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
 11-59 3.04e-07

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 47.12  E-value: 3.04e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTA--NHKKSMLDkGESSCPVCR 59
Cdd:cd16581    1 EELTCSICYNIFDDPKILPCSHTFCKNCLEKllAASGYYLL-ASLKCPTCR 50
RING-HC_RNF112 cd16538
RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; ...
 11-59 3.46e-07

RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; RNF112, also known as brain finger protein (BFP), zinc finger protein 179 (ZNF179), or neurolastin, is a peripheral membrane protein that is predominantly expressed in the central nervous system and localizes to endosomes. It contains functional GTPase and C3HC4-type RING-HC finger domains and has been identified as a brain-specific dynamin family GTPase that affects endosome size and spine density. Moreover, RNF112 acts as a downstream target of sigma-1 receptor (Sig-1R) regulation and may play a novel role in neuroprotection by mediating the neuroprotective effects of dehydroepiandrosterone (DHEA) and its sulfated analog (DHEAS).


Pssm-ID: 438200 [Multi-domain]  Cd Length: 52  Bit Score: 46.91  E-value: 3.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMldkGESSCPVCR 59
Cdd:cd16538    1 EPPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGC---EPPCCPECR 46
Bbox2 cd19756
B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of ...
 94-127 3.62e-07

B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2).


Pssm-ID: 380814 [Multi-domain]  Cd Length: 39  Bit Score: 46.64  E-value: 3.62e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530395903  94 HCARHGEKLL-LFCQEDGKVICWLCERSQEHRGHH 127
Cdd:cd19756    1 LCPEHPEEPLkLFCETCQELVCVLCLLSGEHRGHK 35
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
 9-59 3.75e-07

RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2.


Pssm-ID: 438411 [Multi-domain]  Cd Length: 72  Bit Score: 47.34  E-value: 3.75e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQAC---LTANH---KKSMLDKGESSCPVCR 59
Cdd:cd16753    2 LESELTCPICLELFEDPLLLPCAHSLCFNCahrILVSHcasNESVESITAFQCPTCR 58
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 15-57 3.78e-07

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 46.99  E-value: 3.78e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKGeSSCPV 57
Cdd:cd16643    4 CPICLMALREPVQTPCGHRFCKACI----LKSIREAG-HKCPV 41
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
 10-64 4.86e-07

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 46.59  E-value: 4.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMldkgESSCPVCR--ISYQP 64
Cdd:cd16568    2 LETQECIICHEYLYEPMVTTCGHTYCYTCLNTWFKSNR----SLSCPDCRtkITTQP 54
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 9-59 4.87e-07

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 438412 [Multi-domain]  Cd Length: 70  Bit Score: 46.90  E-value: 4.87e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLtanHK--KSMLDKGESS-------CPVCR 59
Cdd:cd16754    4 LESELTCPICLELFEDPLLLPCAHSLCFSCA---HRilTSGCASGESIeppsafqCPTCR 60
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 348-475 5.97e-07

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 50.21  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 348 ILGSQSITSGKHYWEVDVSKKT-AWILGVcagfqpdAMCNIEKNENYQPKYGYWVIGLEE--GVKCSAFQDSSFHTPSVP 424
Cdd:cd12901   76 VLGDTLIDGGQHYWEVRAQKDSkAFSVGV-------AYRSLGKFDQLGKTNASWCLHVNNwlQNSFAAKHNNKAKTLDVP 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 425 FivplsviicPDRVGVFLDYEACTVSFFNITNHGfLIYKFShCSFSQPVFP 475
Cdd:cd12901  149 V---------PDRIGVYCDFDEGQLSFYNARTKQ-LLHTFK-MKFTQPVLP 188
RING-HC_BAH1-like cd23127
RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 ...
 12-59 6.40e-07

RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 (BAH1) and similar proteins; This subfamily includes Arabidopsis thaliana BAH1 and BAH1-like. BAH1, also known as protein NITROGEN LIMITATION ADAPTATION (NLA), or RING-type E3 ubiquitin transferase BAH1, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It plays a role in salicylic acid-mediated negative feedback regulation of salicylic acid (SA) accumulation. It may be involved in the overall regulation of SA, benzoic acid and phenylpropanoid biosynthesis. It controls the adaptability to nitrogen limitation by channeling the phenylpropanoid metabolic flux to the induced anthocyanin synthesis. BAH1-like, also known as RING finger protein 178, or RING-type E3 ubiquitin transferase BAH1-like, is a probable E3 ubiquitin-protein ligase. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438489 [Multi-domain]  Cd Length: 74  Bit Score: 47.01  E-value: 6.40e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACltANHKKSML-------DKGESSCPVCR 59
Cdd:cd23127    8 DLTCSICLDTVFDPVALGCGHLFCNSC--ACSAASVLifqglkaAPPEAKCPLCR 60
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
 14-59 8.28e-07

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) in the RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438215 [Multi-domain]  Cd Length: 57  Bit Score: 46.13  E-value: 8.28e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDkGESSCPVCR 59
Cdd:cd16553    3 ECPICLQDARFPVETNCGHLFCGPCIITYWRHGSWL-GAVSCPVCR 47
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
 9-59 1.06e-06

RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger.


Pssm-ID: 438285 [Multi-domain]  Cd Length: 63  Bit Score: 45.96  E-value: 1.06e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMLDKGES--SCPVCR 59
Cdd:cd16623    5 LEMEATCPICLDFFSHPISLSCAHIFCFDCI----QKWMTKREDSilTCPLCR 53
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
 12-59 1.13e-06

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 45.85  E-value: 1.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTanhkKSMLDKGEssCPVCR 59
Cdd:cd16535    1 ELQCSICSELFIEAVTLNCSHSFCSYCIT----EWMKRKKE--CPICR 42
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
 15-59 1.34e-06

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 45.35  E-value: 1.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTAnhkksMLDkGESSCPVCR 59
Cdd:cd16561    5 CSICLEDLNDPVKLPCDHVFCEECIRQ-----WLP-GQMSCPLCR 43
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 313-475 1.82e-06

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 48.23  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 313 ISEDKRQVSSPKP-QIIYGARGTRYQTFVNfnyctgILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMcniEKNE 391
Cdd:cd12890   24 LTEDNRKVTNTTPwEHPYPDHPERFEHWRQ------VLSQQSLYLGRYYFEVEISGEGTYVGLTYKSIDRKGS---ESNS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 392 NYQPKYGYWVIGLEeGVKCSAFQ-DSSFHTPSVPFivplsviicpDRVGVFLDYEACTVSFFNITNHGF-LIYKFShCSF 469
Cdd:cd12890   95 CISGNNFSWCLQWN-GKEFSAWHsDVETPLKKGPF----------TRLGIYLDYPGGTLSFYGVEDDGMtLLHKFQ-CKF 162


                 ....*.
gi 530395903 470 SQPVFP 475
Cdd:cd12890  163 TEPLYP 168
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
 10-62 1.95e-06

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 438372 [Multi-domain]  Cd Length: 56  Bit Score: 44.73  E-value: 1.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  10 KEEVTCPICLELLTQPLSL-DCGHSFCQACLtanhKKSMLDKgeSSCPVCRISY 62
Cdd:cd16712    1 QEEDECPICMDRISNKKVLpKCKHVFCAACI----DKAMKYK--PVCPVCGTIY 48
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
 14-59 2.24e-06

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 438121 [Multi-domain]  Cd Length: 44  Bit Score: 44.20  E-value: 2.24e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  14 TCPICLELLTQP----LSLDCGHSFCQACLTAnhkksmldKGESSCPVCR 59
Cdd:cd16457    2 TCPVCLERMDESvsgiLTILCNHSFHCSCLSK--------WGDSSCPVCR 43
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
 13-68 2.69e-06

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 44.54  E-value: 2.69e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLtaNHKKSMLDKGESSCPVCRISYQPENIR 68
Cdd:cd16536    1 PQCPICLEPPVAPRITRCGHIFCWPCI--LRYLSLSEKKWRKCPICFESIHKKDLR 54
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
 14-59 2.78e-06

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 44.22  E-value: 2.78e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLtanhkkSMLDKGESSCPVCR 59
Cdd:cd16532    2 ICPICQDEFKDPVVLRCKHIFCEDCV------SEWFERERTCPLCR 41
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 11-59 2.93e-06

first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.


Pssm-ID: 438500 [Multi-domain]  Cd Length: 48  Bit Score: 44.36  E-value: 2.93e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLtanhKKSMlDKGESSCPVCR 59
Cdd:cd23138    1 DELNCSFCMQLPERPVTTPCGHNFCLKCF----QKWM-GQGKKTCGTCR 44
RING-HC_LONFs_rpt1 cd16513
first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 11-59 4.02e-06

first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the first RING-HC finger.


Pssm-ID: 438176 [Multi-domain]  Cd Length: 47  Bit Score: 43.84  E-value: 4.02e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLtaNHKKSmldkgeSSCPVCR 59
Cdd:cd16513    1 DLLSCPLCRGLLFEPVTLPCGHTFCKRCL--ERDPS------SRCRLCR 41
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
 9-59 4.36e-06

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438187 [Multi-domain]  Cd Length: 53  Bit Score: 43.95  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQA-CLtanhkKSMLDKGESS--CPVCR 59
Cdd:cd16524    2 IEQLLTCPICLDRYRRPKLLPCQHTFCLSpCL-----EGLVDYVTRKlkCPECR 50
RING-HC_ORTHRUS_rpt2 cd23139
second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 12-41 4.70e-06

second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the second one.


Pssm-ID: 438501 [Multi-domain]  Cd Length: 72  Bit Score: 44.37  E-value: 4.70e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLTA 41
Cdd:cd23139    5 EFGCQICKKVLSLPVSTPCGHNFCKACLEA 34
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
 11-59 5.10e-06

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 438216 [Multi-domain]  Cd Length: 59  Bit Score: 43.84  E-value: 5.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  11 EEVTCPICLELLTQPL-SLDCGHSFCQACL---TANHKKSMLdkgessCPVCR 59
Cdd:cd16554    1 ESLTCPVCLDLYYDPYmCYPCGHIFCEPCLrqlAKSSPKNTP------CPLCR 47
Bbox2_TRIM35_C-IV cd19777
B-box-type 2 zinc finger found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 95-126 5.33e-06

B-box-type 2 zinc finger found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380835 [Multi-domain]  Cd Length: 44  Bit Score: 43.24  E-value: 5.33e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19777    6 CRLHGETLKLFCLDDKELLCCACQSSKQHQGH 37
RING-HC_RNF114 cd16540
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ...
 14-59 5.36e-06

RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in the immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438202 [Multi-domain]  Cd Length: 46  Bit Score: 43.21  E-value: 5.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16540    3 TCPVCLEIFETPVRVPCGHVFCNACL-----QECLKPKKPVCAVCR 43
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 14-62 5.84e-06

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438211 [Multi-domain]  Cd Length: 47  Bit Score: 43.26  E-value: 5.84e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  14 TCPICLELLTQPLSL-DCGHSFCQACLtanhkKSMLDKGESSCPVCRISY 62
Cdd:cd16549    3 SCPICLEVYHKPVVItSCGHTFCGECL-----QPCLQVASPLCPLCRMPF 47
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 130-175 6.00e-06

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 45.23  E-value: 6.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530395903  130 LTEEVArEYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQ 175
Cdd:pfam12325  69 LEKELK-ELEQRYETTLELLGEKSEEVEELKADVEDLKEMYREQVQ 113
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
 12-59 6.69e-06

RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain.


Pssm-ID: 438213 [Multi-domain]  Cd Length: 55  Bit Score: 43.30  E-value: 6.69e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGES--SCPVCR 59
Cdd:cd16551    1 ELTCAGCLEVPVEPATLPCGHTLCRGCA-----NRALDAAEAgpTCPRCR 45
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 15-59 7.02e-06

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 43.06  E-value: 7.02e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16509    6 CAICLDSLTNPVITPCAHVFCRRCI-----CEVIQREKAKCPMCR 45
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 14-59 7.29e-06

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 43.16  E-value: 7.29e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  14 TCPICLE-LLTQPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16564    2 ECPVCYEdFDDAPRILSCGHSFCEDCL-----VKQLVSMTISCPICR 43
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
 11-69 8.25e-06

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 43.37  E-value: 8.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903  11 EEVTCPICLELLT-----QPLSLDCGHSFCQACLtanhkKSMLDKGESSCPVCRISYQPENIRP 69
Cdd:cd16450    1 EGNTCPICFEPWTssgehRLVSLKCGHLFGYSCI-----EKWLKGKGKKCPQCNKKAKRSDIRP 59
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
 13-59 9.17e-06

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis. Functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438237 [Multi-domain]  Cd Length: 54  Bit Score: 42.99  E-value: 9.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLtanHK--KSMLDKGESS-------CPVCR 59
Cdd:cd16575    1 LTCPICLELFEDPLLLPCAHSLCFNCA---HRilVSHCASNESVesitafqCPTCR 53
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 11-59 9.51e-06

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 42.78  E-value: 9.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICLELLTQPLSLD-CGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16620    2 DELKCPICKDLMKDAVLTPcCGNSFCDECI-----RTALLEEDFTCPTCK 46
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 15-78 1.16e-05

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 47.69  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903   15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKgESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:TIGR00599  29 CHICKDFFDVPVLTSCSHTFCSLCI-----RRCLSN-QPKCPLCRAEDQESKLRSNWLVSEIVE 86
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
 15-59 1.22e-05

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 438208 [Multi-domain]  Cd Length: 50  Bit Score: 42.37  E-value: 1.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACL--TANHKKsmldkgesSCPVCR 59
Cdd:cd16546    3 CPICLQTCIHPVKLPCGHIFCYLCVkgVAWQSK--------RCALCR 41
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 342-475 1.26e-05

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 45.63  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYWEVDVSkkTAWilgVCAGFqpdamcniekNENYQPKYG----YWVIG-------LE-EGVK 409
Cdd:cd13737   38 FNHWPQVLCTRSLCEGCHYWEAEVS--NSW---VCLGV----------TYSYSHPTGksciFYLIGrnpyswcLEwDSLK 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903 410 CSAFQD--------SSFHTpsvpfivplsviicpdrVGVFLDYEACTVSFFNITNHGFLIYKFShCSFSQPVFP 475
Cdd:cd13737  103 FSVWHNniqtvvhgSYYKT-----------------IGVLLDYAAGSLTFYGVANTMNLIYRFL-TTFTEPLYP 158
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
 14-59 1.29e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger.


Pssm-ID: 438299 [Multi-domain]  Cd Length: 42  Bit Score: 42.00  E-value: 1.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgessCPVCR 59
Cdd:cd16637    3 TCHICLQPLVEPLDTPCGHTFCYKCLTNYLKIQQC------CPLDR 42
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
 12-60 1.65e-05

RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438193 [Multi-domain]  Cd Length: 66  Bit Score: 42.64  E-value: 1.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  12 EVTCPICLELLTQPL-SLDCGHSFCQACLTanhkkSMLDKGESSCPVCRI 60
Cdd:cd16531    1 ELMCPICLGIIKNTMtVKECLHRFCAECIE-----KALRLGNKECPTCRK 45
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
 10-39 2.18e-05

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 438419 [Multi-domain]  Cd Length: 56  Bit Score: 41.82  E-value: 2.18e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACL 39
Cdd:cd16763    1 EEDLTCSVCYSLFEDPRVLPCSHTFCRNCL 30
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
 342-477 2.24e-05

PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation.


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 44.82  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 342 FNYCTGILGSQSITSGKHYW--EVDVSKKTAWILGVCAGfqpDAMcniEKNE-NYQPKYGYWVIGLEEGVkCSAFqdSSF 418
Cdd:cd15827   40 FDRATCVLAHDGFTGGRHTWvvSVDLAHGGSCTVGVVSE---DVR---RKGElRLRPEEGVWAVRLAWGF-VSAL--GSF 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530395903 419 HTpsvpfivPLSVIICPDRVGVFLDYEACTVSFFNITNHGfLIYKFShCSFSQPVFPYL 477
Cdd:cd15827  111 PT-------RLALEEQPRQVRVSLDYEVGWVTFVNAVTQE-PIYTFT-ASFTQKVFPFF 160
Bbox2_TRIM44 cd19784
B-box-type 2 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar ...
 95-126 2.75e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 44 (TRIM44) and similar proteins; TRIM44, also termed protein DIPB, functions as a critical regulator in tumor metastasis and progression. TRIM44 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380842 [Multi-domain]  Cd Length: 39  Bit Score: 41.30  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19784    3 CPEHGQELSLYCKEDEKIICVLCAVIGAHRQH 34
Bbox2_TRIM20 cd19771
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM20 and similar ...
 95-126 2.96e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM20 and similar proteins; TRIM20, also termed Pyrin, or Marenostrin (MEFV), is involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. TRIM20 belongs to unclassified TRIM family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a pyrin domain, a Bbox2 zinc finger, and a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380829 [Multi-domain]  Cd Length: 39  Bit Score: 40.92  E-value: 2.96e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19771    3 CKLHLEQLKLFCEDHREPICLICQLSQEHQGH 34
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
 10-59 3.17e-05

RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers protein 20 (IRC20) and similar proteins; IRC20 is an uncharacterized ATP-dependent helicase that is probably involved in a pathway contributing to genomic integrity. IRC20 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 41.35  E-value: 3.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKgESSCPVCR 59
Cdd:cd23135    1 KQKLSCSICFSEIRSGAILKCGHFFCLSCI-----ASWLRE-KSTCPLCK 44
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
 15-59 3.19e-05

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 438403 [Multi-domain]  Cd Length: 45  Bit Score: 41.32  E-value: 3.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanHKKSMLDKGESSCPVCR 59
Cdd:cd16745    3 CNICLDLAQDPVVTLCGHLFCWPCL---HKWLRRQSSQPECPVCK 44
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
 12-62 4.01e-05

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 41.25  E-value: 4.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903  12 EVTCPICLELLTQPLSLD-CGHSFCQACLTANHKKsmldkgESSCPVCRISY 62
Cdd:cd16711    1 EETCPICLGEIQNKKTLDkCKHSFCEDCITRALQV------KKACPMCGEFY 46
mRING-HC-C3HC3D_LNX2 cd16780
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); ...
 11-39 4.32e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); LNX2, also known as numb-binding protein 2, or PDZ domain-containing RING finger protein 1 (PDZRN1), is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. It interacts with contactin-associated protein 4 (Caspr4, also known as CNTNAP4) in a PDZ domain-dependent manner, which modulates the proliferation and neuronal differentiation of neural progenitor cells (NPCs). LNX2 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAF motif for Numb/ Numblike-LNX interaction, and four PDZ domains necessary for the binding of substrates, including ErbB2, RhoC, the presynaptic protein CAST, the melanoma/cancer-testis antigen MAGEB18 and several proteins associated with cell junctions, such as JAM4 and the Coxsackievirus and adenovirus receptor (CAR).


Pssm-ID: 319694 [Multi-domain]  Cd Length: 45  Bit Score: 40.63  E-value: 4.32e-05
                         10        20
                 ....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACL 39
Cdd:cd16780    2 DDLVCHICLQPLLQPLDTPCGHTFCFKCL 30
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
 14-59 4.66e-05

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438275 [Multi-domain]  Cd Length: 46  Bit Score: 40.80  E-value: 4.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgesSCPVCR 59
Cdd:cd16613    2 TCICCQELVYKPITTPCKHNICKSCLQRSFKAEVY-----TCPACR 42
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-240 5.30e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 130 LTEEVAREYQV-----KLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRdildwEESNELQNLE 204
Cdd:COG1196  283 LEEAQAEEYELlaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-----EAEEELEEAE 357

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530395903 205 KEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
RING-HC_RNF183-like cd16556
RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar ...
 15-59 5.77e-05

RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins; RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438218 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 5.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  15 CPICLELLTQ----PLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCR 59
Cdd:cd16556    3 CSICFSSYDNtfktPKLLDCGHTFCLECLARLSLASPPQAERVPCPLCR 51
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
 11-59 6.06e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and similar proteins; Tripartite motif-containing proteins TRIM9 and TRIM67 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.


Pssm-ID: 438238 [Multi-domain]  Cd Length: 42  Bit Score: 40.47  E-value: 6.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  11 EEVTCPICLELLTQPLSLDCGHSFCQACLTANhkksmldkgESSCPVCR 59
Cdd:cd16576    2 EELKCPVCGSLFTEPVILPCSHNLCLGCALNI---------QLTCPICH 41
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 15-57 6.53e-05

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 40.41  E-value: 6.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTanhkksmlDKGESSCPV 57
Cdd:cd16644    8 CPLCQRVFKDPVITSCGHTFCRRCAL--------TAPGEKCPV 42
zf-RING_2 pfam13639
Ring finger domain;
14-59 7.08e-05

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 40.08  E-value: 7.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530395903   14 TCPICLELLT---QPLSLDCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:pfam13639   2 ECPICLEEFEegdKVVVLPCGHHFHRECLDKWLRSS------NTCPLCR 44
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
15-58 7.20e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 40.11  E-value: 7.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530395903   15 CPICLELLTQPL-SLDCGHSFCQACLtanhkKSMLDKGeSSCPVC 58
Cdd:pfam13923   2 CPICMDMLKDPStTTPCGHVFCQDCI-----LRALRAG-NECPLC 40
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
 14-59 7.31e-05

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 438201 [Multi-domain]  Cd Length: 54  Bit Score: 40.27  E-value: 7.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:cd16539    7 ACFICRKPFKNPVVTKCGHYFCEKCALKHYRKS------KKCFVCG 46
RING-HC_RING1 cd16739
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ...
 12-59 7.54e-05

RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438397 [Multi-domain]  Cd Length: 70  Bit Score: 40.83  E-value: 7.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  12 EVTCPICLELLTQPLSL-DCGHSFCQACLTanhkkSMLDKGESSCPVCR 59
Cdd:cd16739    3 ELMCPICLDMLKNTMTTkECLHRFCSDCIV-----TALRSGNKECPTCR 46
mRING-HC-C3HC3D_Roquin1 cd16781
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1; Roquin-1, also known as ...
 11-46 8.05e-05

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1; Roquin-1, also known as RING finger and C3H zinc finger protein 1 (RC3H1), or RING finger protein 198 (RNF198), is a ubiquitously expressed RNA-binding protein essential for degradation of inflammation-related mRNAs and maintenance of immune homeostasis. It is localized in cytoplasmic granules and binds to the 3' untranslated region (3'UTR) of inducible costimulator (Icos) mRNA to post-transcriptionally repress its expression. Roquin-1 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and post-transcriptionally regulates A20 mRNA and modulates the activity of the IKK/NF-kappaB pathway. Moreover, Roquin-1 shares functions with its paralog Roquin-2 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-1 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger that is involved in RNA recognition, typically contacting AU-rich elements. In addition, both N- and C-terminal to the ROQ domain are combined to form a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain that is highly likely to function as an RNA-binding domain.


Pssm-ID: 438436 [Multi-domain]  Cd Length: 49  Bit Score: 40.38  E-value: 8.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICL----ELLTQPLSLDCGHSFCQACLTANHKKS 46
Cdd:cd16781    5 DFLSCPICTqtfdETIRKPISLGCGHTVCKMCLNKLHRKA 44
Bbox2_TRIM72_C-IV cd19797
B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 93-133 8.22e-05

B-box-type 2 zinc finger found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis via targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380855 [Multi-domain]  Cd Length: 42  Bit Score: 39.96  E-value: 8.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530395903  93 DHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEE 133
Cdd:cd19797    1 GHCEEHLDPLSVYCEQDRALICGVCASLGKHKGHNIITAAE 41
mRING-HC-C3HC3D_LNX1 cd16779
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); ...
 12-40 9.59e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); LNX1, also known as numb-binding protein 1 or PDZ domain-containing RING finger protein 2, is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX1 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAY motif for Numb-LNX interaction, and four PDZ domains necessary for the binding of substrates, including CAR, ErbB2, SKIP, JAM4, CAST, c-Src, Claudins, RhoC, KCNA4, PAK6, PLEKHG5, PKC-alpha1, TYK2, PDZ-binding kinase (PBK), LNX2, and itself.


Pssm-ID: 438435 [Multi-domain]  Cd Length: 42  Bit Score: 39.79  E-value: 9.59e-05
                         10        20
                 ....*....|....*....|....*....
gi 530395903  12 EVTCPICLELLTQPLSLDCGHSFCQACLT 40
Cdd:cd16779    1 DLICHICLQALIQPLDTPCGHTYCTLCLT 29
RING-HC_MuRF2 cd16760
RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
 10-59 1.27e-04

RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins; MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and is also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signaling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 438417 [Multi-domain]  Cd Length: 64  Bit Score: 39.98  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903  10 KEEVTCPICLELLTQPLS-LDCGHSFCQAC-----------LTANHKKSMLDKGESSCPVCR 59
Cdd:cd16760    1 EKQLICPICLEMFTKPVViLPCQHNLCRKCandifqasnpyLPTRGGTTVASGGRFRCPSCR 62
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 142-255 1.35e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.90  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 142 LQAALEMLRQK----QQEAEELEADIREekasWKTQIQYDKTNVLADFEQLRDILDWEES----NELQNLEKEEEDILKS 213
Cdd:cd22656  119 IKALLDDLLKEakkyQDKAAKVVDKLTD----FENQTEKDQTALETLEKALKDLLTDEGGaiarKEIKDLQKELEKLNEE 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903 214 LTNsetEMVQQTQSLRELISDLEH------RLQGSVMELLQGVDGVIK 255
Cdd:cd22656  195 YAA---KLKAKIDELKALIADDEAklaaalRLIADLTAADTDLDNLLA 239
RING-HC_RING2 cd16740
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ...
 8-80 1.44e-04

RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins; RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438398 [Multi-domain]  Cd Length: 77  Bit Score: 40.46  E-value: 1.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530395903   8 NVKEEVTCPICLELLTQPLSL-DCGHSFCQACLTanhkkSMLDKGESSCPVCRISY-QPENIRPNRHVANIVEKL 80
Cdd:cd16740    8 SLHSELMCPICLDMLKNTMTTkECLHRFCADCII-----TALRSGNKECPTCRKKLvSKRSLRPDPNFDALISKI 77
RING-HC_TRIM36_C-I cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
 10-39 1.48e-04

RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438414 [Multi-domain]  Cd Length: 49  Bit Score: 39.51  E-value: 1.48e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACL 39
Cdd:cd16756    1 ERELICPSCKELFTHPLILPCQHSVCHKCV 30
Bbox2_TRIM60-like cd19791
B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM60, TRIM61, ...
 95-127 1.49e-04

B-box-type 2 zinc finger found in tripartite motif-containing proteins, TRIM60, TRIM61, TRIM75 and similar proteins; This family includes a group of tripartite motif-containing proteins, including TRIM60, TRIM61 and TRIM75. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. TRIM60 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM61 is closely related to TRIM60, but its biological function remains unclear. TRIM75 could be the product of a pseudogene. Its biological function remains unclear. TRIM60 and TRIM75 belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380849 [Multi-domain]  Cd Length: 39  Bit Score: 39.06  E-value: 1.49e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHH 127
Cdd:cd19791    3 CEKHNQPLTKFCKKDLEPLCPQCSQSTDHQHHV 35
RING-HC_RBR_TRIAD1 cd16773
RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 ...
 13-38 1.49e-04

RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1); TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is an RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48, as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. It functions as a regulator of endosomal transport and is required for the proper function of multivesicular bodies. It also acts as a novel ubiquitination target for proteasome-dependent degradation by murine double minute 2 (MDM2). As a proapoptotic protein, TRIAD1 promotes p53 activation, and inhibits MDM2-mediated p53 ubiquitination and degradation. Furthermore, TRIAD1 can inhibit the ubiquitination and proteasomal degradation of growth factor independence 1 (Gfi1), a transcriptional repressor essential for the function and development of many different hematopoietic lineages. TRIAD1 contains an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438429 [Multi-domain]  Cd Length: 54  Bit Score: 39.64  E-value: 1.49e-04
                         10        20
                 ....*....|....*....|....*...
gi 530395903  13 VTCPICLELLTQP--LSLDCGHSFCQAC 38
Cdd:cd16773    1 VTCGVCCEDVPKDelFSLACGHYFCNDC 28
zf-B_box pfam00643
B-box zinc finger;
90-128 1.58e-04

B-box zinc finger;


Pssm-ID: 459886 [Multi-domain]  Cd Length: 42  Bit Score: 38.99  E-value: 1.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530395903   90 QKVDHCARHG-EKLLLFCQEDGKVICWLCERSqEHRGHHT 128
Cdd:pfam00643   1 SKERLCPEHEeEPLTLYCNDCQELLCEECSVG-EHRGHTV 39
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
 15-69 1.82e-04

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 438190 [Multi-domain]  Cd Length: 52  Bit Score: 39.13  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLT--ANHKksmldkgeSSCPVCRISYQPENIRP 69
Cdd:cd16527    3 CSLCLEERRHPTATPCGHLFCWSCITewCNEK--------PECPLCREPFQPQRLVP 51
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 357-452 1.85e-04

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 41.26  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 357 GKHYWEVDV--SKKTAWILGVC-AGFQPDAMCNIEKNENYqpkygyWVIGLEEGVKCSAFQDSSFHTPSVPfivplsvii 433
Cdd:cd11709    1 GKWYWEVRVdsGNGGLIQVGWAtKSFSLDGEGGVGDDEES------WGYDGSRLRKGHGGSSGPGGRPWKS--------- 65

                         90
                 ....*....|....*....
gi 530395903 434 cPDRVGVFLDYEACTVSFF 452
Cdd:cd11709   66 -GDVVGCLLDLDEGTLSFS 83
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
 12-62 1.91e-04

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 39.19  E-value: 1.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  12 EVTCPICLELLTQPLS-LD-CGHSFCQACLtanHKKSmldKGESSCPVCRISY 62
Cdd:cd16574    1 DSSCPICLDRFENEKAfLDgCFHAFCFTCI---LEWS---KVKNECPLCKQPF 47
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 15-67 1.93e-04

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 43.34  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKgessCPVCRISYQPENI 67
Cdd:COG5574  218 CFLCLEEPEVPSCTPCGHLFCLSCLLISWTKKKYEF----CPLCRAKVYPKKV 266
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 10-61 2.31e-04

RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9, human ortholog of rat Spring, also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducin repeat-containing protein (beta-TrCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulates nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and the exocytic soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438413 [Multi-domain]  Cd Length: 55  Bit Score: 39.24  E-value: 2.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACltANHKKSMLDKGES-----SCPVCRIS 61
Cdd:cd16755    1 EEELKCPVCGSFYREPIILPCSHNLCLAC--ARNILVQTPEAESpqsclTCPQCHRS 55
mRING-HC-C3HC3D_Roquin cd16638
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar ...
 14-45 2.47e-04

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar proteins; The ROQUIN family includes Roquin-1, Roquin-2, and similar proteins, which localize to the cytoplasm and upon stress, are concentrated in stress granules. They may play essential roles in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. They function as E3 ubiquitin ligases consisting of an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 activity, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger involved in RNA recognition.


Pssm-ID: 438300 [Multi-domain]  Cd Length: 44  Bit Score: 38.48  E-value: 2.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530395903  14 TCPICL----ELLTQPLSLDCGHSFCQACLTANHKK 45
Cdd:cd16638    3 SCPVCTnefdGTQRKPISLGCGHTVCKTCLSKLHRK 38
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 15-59 2.57e-04

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 38.54  E-value: 2.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903  15 CPICLELLTQPLS---LDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16448    1 CVICLEEFEEGDVvrlLPCGHVFHLACI-----LRWLESGNNTCPLCR 43
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
 14-59 2.64e-04

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 38.69  E-value: 2.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLTAnHKKSMLDKGESSCPVCR 59
Cdd:cd16579    6 RCPGCKAEYKCPKLLPCLHTVCSGCLEA-LAEQASETTEFQCPICK 50
RING-HC_MuRF_C-II cd16577
RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55 ...
 15-59 2.71e-04

RING finger, HC subclass, found in muscle-specific RING finger proteins TRIM63/MuRF-1, TRIM55/MuRF-2 and TRIM54/MuRF-3; This subfamily corresponds to a group of striated muscle-specific tripartite motif (TRIM) proteins, including TRIM63/MuRF-1, TRIM55/MuRF-2, and TRIM54/MuRF-3, which function as E3 ubiquitin ligases in ubiquitin-mediated muscle protein turnover. They are tightly developmentally regulated in skeletal muscle and associate with different cytoskeleton components, such as microtubules, Z-disks and M-bands, as well as with metabolic enzymes and nuclear proteins. They also cooperate with diverse proteins implicated in selective protein degradation by the proteasome and autophagosome, and target proteins of metabolic regulation, sarcomere assembly and transcriptional regulation. Moreover, MURFs display variable fibre-type preferences. TRIM63/MuRF-1 is predominantly fast (type II) fibre-associated in skeletal muscle. TRIM55/MuRF-2 is predominantly slow-fibre associated. TRIM54/MuRF-3 is ubiquitously present. They play an active role in microtubule-mediated sarcomere assembly. MuRFs belong to the C-II subclass of the TRIM family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain positioned C-terminal to the RBCC domain. They also harbor a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 438239 [Multi-domain]  Cd Length: 56  Bit Score: 38.72  E-value: 2.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  15 CPICLELLTQPLS-LDCGHSFCQACL--------TANHKKSMLDKGESSCPVCR 59
Cdd:cd16577    3 CPICLEMFTKPVViLPCQHNLCRKCAndifqarnPYWPTTTMGSGGRFRCPSCR 56
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
132-240 2.71e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 132 EEVAREYQvKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQY--------DKTNVLADF--------EQLRDILDWE 195
Cdd:COG4717   84 EEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELperleeleERLEELRELE 162

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903 196 E-----SNELQNLEKEEEDILKSLTNSE----TEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG4717  163 EeleelEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELE 216
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
 15-66 2.94e-04

RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438482 [Multi-domain]  Cd Length: 54  Bit Score: 38.67  E-value: 2.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLS--LDCGHSFCQACLTANHKKSmldkGESSCPVCRI-SYQPEN 66
Cdd:cd23120    4 CPICLEEMNSGTGylADCGHEFHLTCIREWHNKS----GNLDCPICRVeSLLLED 54
RING-HC_LNX4 cd16719
RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ ...
 9-39 3.08e-04

RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438379 [Multi-domain]  Cd Length: 53  Bit Score: 38.76  E-value: 3.08e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACL 39
Cdd:cd16719    1 VDPDLKCKLCGKVLEEPLSTPCGHVFCAGCL 31
RING-HC_GEFO-like cd16507
RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange ...
 14-59 3.35e-04

RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange factor O (RasGEFO) and similar proteins; RasGEFO, also known as RasGEF domain-containing protein O, functions as a Ras guanine-nucleotide exchange factor (RasGEFs), activating Ras by catalyzing the replacement of GDP with GTP. RasGEFs are particularly important for signaling in development and chemotaxis in many organisms, including Dictyostelium. RasGEFO contains a C3HC4-type RING-HC finger that may be responsible for E3 ubiquitin ligase activity.


Pssm-ID: 438170 [Multi-domain]  Cd Length: 58  Bit Score: 38.87  E-value: 3.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  14 TCPICLELLTQPLSLD-CGHSFCQACLTanhkkSMLDKgeSSCPVCR 59
Cdd:cd16507   11 TCGICQNLFKDPNTLIpCGHAFCLDCLT-----TNASI--KNCIQCK 50
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
 13-59 3.52e-04

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 38.54  E-value: 3.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903  13 VTCPICLELLTQ----PLSLDCGHSFCQACLTANHKKSMLDKgeSSCPVCR 59
Cdd:cd16587    1 LECPICLESFDEgqlrPKLLHCGHTICEQCLEKLLASLSING--VRCPFCR 49
RING-HC_SpRad8-like cd16572
RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) ...
 15-68 4.43e-04

RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) and similar proteins; SpRad8 is a conserved protein homologous to Saccharomyces cerevisiae DNA repair protein Rad5 and human helicase-like transcription factor (HLTF) that is required for error-free postreplication repair by contributing to polyubiquitylation of PCNA. SpRad8 contains a C3HC4-type RING-HC finger responsible for the E3 ubiquitin ligase activity, a SNF2-family helicase domain including an ATP binding site, and a family-specific HIRAN domain (HIP116, Rad5p N-terminal domain) that contributes to nuclear localization.


Pssm-ID: 438234 [Multi-domain]  Cd Length: 61  Bit Score: 38.26  E-value: 4.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530395903  15 CPICLELLTQPLSL-DCGHSFCQACLtANHKKSMLDKGESS-CPVCRisyQPENIR 68
Cdd:cd16572    7 CPICAEEPISELALtRCWHSACKDCL-LDHIEFQKSKNEVPlCPTCR---QPINEQ 58
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
 15-59 4.47e-04

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 38.05  E-value: 4.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanHKKSMLDKGESSCPVCR 59
Cdd:cd16534    3 CNICLDTASDPVVTMCGHLFCWPCL---YQWLETRPDRQTCPVCK 44
RING-HC_TIF1_C-VI cd16585
RING finger, HC subclass, found in the transcriptional inknown asiary factor 1 (TIF1) ...
 14-59 5.13e-04

RING finger, HC subclass, found in the transcriptional inknown asiary factor 1 (TIF1) subfamily and similar proteins; The TIF1 subfamily of transcriptional cofactors containing RING-HC fingers includes TIF1alpha (TRIM24), TIF1beta (TRIM28), and TIF1gamma (TRIM33), which belong to the C-VI subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatin proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs). TIF1delta (TRIM66) doesn't have a RING-HC finger and is not included in this model.


Pssm-ID: 438247 [Multi-domain]  Cd Length: 62  Bit Score: 38.34  E-value: 5.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  14 TCPICLELLT--QPLSLDCGHSFCQACLTANHKKSMLDKGESS---------CPVCR 59
Cdd:cd16585    3 TCAVCKQSFQsrEPKLLPCLHSFCKRCLPPADRAAANPSPSGGaagqvgvirCPVCK 59
RING-HC_MuRF1 cd16759
RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
 10-59 5.24e-04

RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins; MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319673 [Multi-domain]  Cd Length: 63  Bit Score: 38.47  E-value: 5.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903  10 KEEVTCPICLELLTQPLS-LDCGHSFCQACL-----------TANHKKSMLDKGESSCPVCR 59
Cdd:cd16759    1 EKQLICPICLEMFTKPVViLPCQHNLCRKCAndifqaanpywQSRGTSMLGSGGRFRCPSCR 62
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
 15-59 5.27e-04

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438399 [Multi-domain]  Cd Length: 58  Bit Score: 38.33  E-value: 5.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKsmldkgESSCPVCR 59
Cdd:cd16741   17 CAICQAEFRKPILLICQHVFCEECISLWFNR------EKTCPLCR 55
RING-HC_TRIM46_C-I cd16757
RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar ...
 9-40 5.41e-04

RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438415 [Multi-domain]  Cd Length: 43  Bit Score: 37.49  E-value: 5.41e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACLT 40
Cdd:cd16757    1 MERELLCPVCKEMYKQPLVLPCMHNVCQVCAS 32
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 15-61 5.78e-04

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 38.05  E-value: 5.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530395903  15 CPICLELL-TQPLSLDCGHSFCQACLtanhKKSMLDKgeSSCPVCRIS 61
Cdd:cd16529    7 CPICFEYFnTAMMITQCSHNYCSLCI----RRFLSYK--TQCPTCRAA 48
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
15-78 5.85e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 42.00  E-value: 5.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKgESSCPVCRISYQPENIRPNRHVANIVE 78
Cdd:COG5432   28 CRICDCRISIPCETTCGHTFCSLCI-----RRHLGT-QPFCPVCREDPCESRLRGSSGSREINE 85
Bbox2_TRIM14 cd19768
B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar ...
 95-135 6.09e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins; TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380826 [Multi-domain]  Cd Length: 44  Bit Score: 37.40  E-value: 6.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLL-LFCQEDGKVICWLCERSQEHRGHHTFLTEEVA 135
Cdd:cd19768    3 CPEHKDRPLeLFCKTCKRCVCALCPILGQHRGHDVRLIDEEA 44
RING-H2_RNF32_rpt1 cd16677
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
 15-59 6.38e-04

first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the first RING-H2 finger.


Pssm-ID: 438339 [Multi-domain]  Cd Length: 49  Bit Score: 37.66  E-value: 6.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLEL--LTQPLSLDCGHSFCQACLTANHKKSmldkGESSCPVCR 59
Cdd:cd16677    2 CPICLEDfgLQQQVLLSCSHVFHRACLESFERFS----GKKTCPMCR 44
RING-HC_TRIM67 cd16758
RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 10-58 6.92e-04

RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also known as TRIM9-like protein (TNL), is selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438416 [Multi-domain]  Cd Length: 57  Bit Score: 37.75  E-value: 6.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACL------TANHKKSMLDKGESSCPVC 58
Cdd:cd16758    1 EEELKCPVCGSLFREPIILPCSHNVCLPCArtiavqTPESEQHLPHSSSITCPQC 55
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 142-240 7.28e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 142 LQAALEMLRQKQQEAEELEADIREEKAsWKTQIQYDKTNVLADFEQLRDILDwEESNELQNLEKEEEDILKSLTNSETEM 221
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAALEAELAELEKEI 92

                         90
                 ....*....|....*....
gi 530395903 222 VQQTQSLRELISDLEHRLQ 240
Cdd:COG4942   93 AELRAELEAQKEELAELLR 111
Bbox2_TRIM40_C-V cd19781
B-box-type 2 zinc finger found in tripartite motif-containing protein 40 (TRIM40) and similar ...
 95-133 8.21e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also termed probable E3 NEDD8-protein ligase, or RING finger protein 35, may function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway. It promotes neddylation of IKBKG/NEMO, stabilizing NFKBIA, and inhibiting NF-kappaB nuclear translocation and activity. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380839 [Multi-domain]  Cd Length: 44  Bit Score: 37.01  E-value: 8.21e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEE 133
Cdd:cd19781    5 CQLHEKKVEWFCEEDQVLLCEECLKSPEHQSHHVLTIED 43
Bbox2_TRIM65-like cd19793
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and ...
 95-135 8.25e-04

B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and SPRY domain-containing protein (BSPRY) and similar proteins; The family includes TRIM65 and BSPRY. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380851  Cd Length: 43  Bit Score: 37.29  E-value: 8.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVA 135
Cdd:cd19793    3 CPEHGRELELYCRTEKRCVCAQCASKGECRGHRVTLLEERA 43
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
 10-59 8.30e-04

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It is encoded by the gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438424 [Multi-domain]  Cd Length: 48  Bit Score: 37.29  E-value: 8.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgESSCPVCR 59
Cdd:cd16768    2 KQFLVCSICLDRYHNPKVLPCLHTFCERCLQNYIPPQSL---TLSCPVCR 48
RING-HC_UHRF2 cd16770
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
 10-59 8.76e-04

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2, also known as Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438426 [Multi-domain]  Cd Length: 65  Bit Score: 37.87  E-value: 8.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgesSCPVCR 59
Cdd:cd16770    1 EESFLCICCQELVYQPVTTECQHNVCKSCLQRSFKAEVY-----TCPACR 45
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
 13-59 8.76e-04

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) by interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifier (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438195 [Multi-domain]  Cd Length: 57  Bit Score: 37.57  E-value: 8.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  13 VTCPICLELLTQ-------PLSLDCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:cd16533    4 VSCPICMDGYSEivqsgrlIVSTECGHVFCSQCLRDSLKNA------NTCPTCR 51
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 142-240 9.64e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 142 LQAALEMLRQKQQEAEELEADIREEKASWKTQIQydktnvladfEQLrdildwEESNELQNLEKEEEDILKSLTNSET-- 219
Cdd:COG4942  148 RREQAEELRADLAELAALRAELEAERAELEALLA----------ELE------EERAALEALKAERQKLLARLEKELAel 211

                         90       100
                 ....*....|....*....|....*.
gi 530395903 220 -----EMVQQTQSLRELISDLEHRLQ 240
Cdd:COG4942  212 aaelaELQQEAEELEALIARLEAEAA 237
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
 11-59 1.07e-03

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 37.25  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  11 EEVTCPICLE------LLTQplsLDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16473    3 ECEECAICLEnyqngdLLRG---LPCGHVFHQNCI-----DVWLERDNHCCPVCR 49
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
 13-66 1.08e-03

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438246 [Multi-domain]  Cd Length: 56  Bit Score: 37.27  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLTanhkkSMLDKGESSCPVCRIS-YQPEN 66
Cdd:cd16584    2 LACKICLEQLRAPKTLPCLHTYCQDCLA-----QLADGGRVRCPECRETvPVPPE 51
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
 13-59 1.15e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438248 [Multi-domain]  Cd Length: 45  Bit Score: 36.66  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  13 VTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgESSCPVCR 59
Cdd:cd16586    2 LSCGICLERYKNPKVLPCLHTFCERCLQNYIPAESL---SLSCPVCR 45
RING-H2_RNF32_rpt2 cd16678
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
 15-62 1.15e-03

second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the second RING-H2 finger.


Pssm-ID: 438340 [Multi-domain]  Cd Length: 61  Bit Score: 37.35  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903  15 CPICLELLTQP--------------LSLDCGHSFCQACLTANHKKSMLDkgESSCPVCRISY 62
Cdd:cd16678    2 CPICLTPLQSSgdssdakrvssrptVLLSCSHVFHATCLEAFEEFSVGE--ELVCPVCRSHY 61
Bbox2_TRIM50-like cd19787
B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
 95-126 1.22e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with the histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. The family also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins and may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by the N-terminal RBCC domains only.


Pssm-ID: 380845 [Multi-domain]  Cd Length: 39  Bit Score: 36.70  E-value: 1.22e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCERSQEHRGH 126
Cdd:cd19787    3 CPHHHNPLSLFCEKDQEVICGLCGLIGSHRQH 34
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
 15-59 1.38e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438400 [Multi-domain]  Cd Length: 67  Bit Score: 37.17  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTAnhkksMLDKgESSCPVCR 59
Cdd:cd16742   16 CAICQAEFREPLILICQHVFCEECLCL-----WFDR-ERTCPLCR 54
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-272 1.44e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   127 HTFLTEEVA--REYQVKLQAALEmLRQKQQEAEELEADIREEKAS----------------WKTQIQYDKTNVLADFEQL 188
Cdd:pfam02463  155 RLEIEEEAAgsRLKRKKKEALKK-LIEETENLAELIIDLEELKLQelklkeqakkaleyyqLKEKLELEEEYLLYLDYLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   189 RDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLREL---ISDLEHRLQGSVMELLQgvdgvIKRTENVTLKKP 265
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEE-----ELKSELLKLERR 308


                   ....*..
gi 530395903   266 ETFPKNQ 272
Cdd:pfam02463  309 KVDDEEK 315
RING-HC_TRIM45_C-VII cd16588
RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar ...
 15-58 1.53e-03

RING finger, HC subclass, found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction through inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-VII subclass of the TRIM (tripartite motif) family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain.


Pssm-ID: 438250 [Multi-domain]  Cd Length: 59  Bit Score: 36.73  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESS----------CPVC 58
Cdd:cd16588    3 CPVCGKLFQEPRLLPCLHTLCSPCLRQLEPFSVCGLRGGDrseksnysvlCPVC 56
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
132-238 1.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 132 EEVAREYQVKLQAALEMLRQKQQEAEELEADIRE----------EKASWKTQIQyDKTNVLADFEQ----LRDILDWEE- 196
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETLEAEIEDlretiaeterEREELAEEVR-DLRERLEELEEerddLLAEAGLDDa 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903 197 -----SNELQNLEKEEEDILKSLTN---SETEMVQQTQSLRELISDLEHR 238
Cdd:PRK02224 308 daeavEARREELEDRDEELRDRLEEcrvAAQAHNEEAESLREDADDLEER 357
zf-RING_5 pfam14634
zinc-RING finger domain;
15-59 1.65e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 36.25  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530395903   15 CPICLELLT---QPLSLDCGHSFCQACLTANHKKSMldkgessCPVCR 59
Cdd:pfam14634   2 CNKCFKELSktrPFYLTSCGHIFCEECLTRLLQERQ-------CPICK 42
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
 14-59 1.77e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 36.36  E-value: 1.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  14 TCPICLELLTQPLSLDCGHSFCQACLtANHKKSmldkgESSCPVCR 59
Cdd:cd23148    5 RCHICKDLLKAPMRTPCNHTFCSFCI-RTHLNN-----DARCPLCK 44
RING-HC_MuRF3 cd16761
RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 15-59 1.82e-03

RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins; MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319675 [Multi-domain]  Cd Length: 59  Bit Score: 36.55  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLTQPLS-LDCGHSFCQACLT-----------ANHKKSMLDKGESSCPVCR 59
Cdd:cd16761    3 CPICLEMFTKPVViLPCQHNLCRKCANdvfqasnplwqSRGSSTVSSGGRFRCPSCR 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-240 1.92e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 133 EVAREYQV------------------KLQAALEMLRQKQQEAEELEADIREEKASWKTQIqydktnvladfEQLRDILDw 194
Cdd:COG1196  210 EKAERYRElkeelkeleaellllklrELEAELEELEAELEELEAELEELEAELAELEAEL-----------EELRLELE- 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903 195 EESNELQNLEKEEEDILKSLTNSEtemvQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLE 319
RING-HC_RNF207 cd16558
RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; ...
 15-58 2.03e-03

RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization in a heat shock protein-dependent manner. RNF207 contains a C3HC4-type RING-HC finger, Bbox 1 and Bbox C-terminal (BBC) domain, as well as a C-terminal non-homologous region (CNHR).


Pssm-ID: 438220 [Multi-domain]  Cd Length: 43  Bit Score: 36.18  E-value: 2.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgesSCPVC 58
Cdd:cd16558    4 CYLCHEQYEHPCLLDCYHTFCASCLRGRAADGRL-----TCPLC 42
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
 10-59 2.59e-03

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438423 [Multi-domain]  Cd Length: 51  Bit Score: 36.15  E-value: 2.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLdkgESSCPVCR 59
Cdd:cd16767    4 KQFLICSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSL---TLSCPVCR 50
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
10-153 2.80e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.00  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  10 KEEVTCPICLELLTQPLSLDCGHSFCQAC---LTANHKKsmldkgeSSCPVCRISYQpENIRPNRHVANIVE----KLRE 82
Cdd:COG5236   59 EENMNCQICAGSTTYSARYPCGHQICHACavrLRALYMQ-------KGCPLCRTETE-AVVFTASSPADITDrrqwKGRE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903  83 VKLSPEGQKVDHCARHGEKLLLFCQEDG-KVICWLCERSQEHRG--HHTFLTEEVAREYQVkLQAALEMLRQKQ 153
Cdd:COG5236  131 EKVGIFYEGEDVRDEMEDLLSFKCPKSKcHRRCGSLKELKKHYKaqHGFVLCSECIGNKKD-FWNEIRLFRSST 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-239 2.96e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   130 LTEEVA--REYQVKLQAALEMLRQKQQEAEELEADIRE----------EKAswkTQIQYDKTNvladfEQLRDILDWEES 197
Cdd:TIGR02169  158 IIDEIAgvAEFDRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrERE---KAERYQALL-----KEKREYEGYELL 229

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 530395903   198 NELQNLEKEEEDILKSLTNSETEMVQqtqsLRELISDLEHRL 239
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEK----LTEEISELEKRL 267
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
 14-59 3.11e-03

RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.


Pssm-ID: 438188 [Multi-domain]  Cd Length: 42  Bit Score: 35.28  E-value: 3.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  14 TCPICLELLTQPLSL-DCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:cd16525    2 TCSLCKGYLIDATTItECLHSFCKSCIVRHLETS------KNCPVCD 42
RING-HC_PCGF5 cd16737
RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, ...
 13-80 3.13e-03

RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, also known as RING finger protein 159 (RNF159), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF5 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438395 [Multi-domain]  Cd Length: 95  Bit Score: 37.04  E-value: 3.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530395903  13 VTCPICLELLTQPLSLD-CGHSFCQACLTANHKKSMLdkgessCPVCRISYQPEN----IRPNRHVANIVEKL 80
Cdd:cd16737   11 ITCRICKGYLIKPTTVTeCLHTFCKSCIVQHFEDSND------CPECGIQVHETNplemLRLDNTLEEIIFKL 77
RING-HC_SH3RF2 cd16749
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and ...
 15-59 3.14e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438407 [Multi-domain]  Cd Length: 46  Bit Score: 35.68  E-value: 3.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  15 CPICLELLTQPLS-LDCGHSFCQACLTANHKKsmldKGESSCPVCR 59
Cdd:cd16749    3 CPVCFEKLDVTAKvLPCQHTFCKPCLQRIFKA----RKELRCPECR 44
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
132-250 3.32e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 132 EEVAREYQvKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDIL 211
Cdd:COG4372  118 EELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530395903 212 KSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGV 250
Cdd:COG4372  197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
 15-69 3.50e-03

RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438401 [Multi-domain]  Cd Length: 54  Bit Score: 35.63  E-value: 3.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanHKKSMLDKGESSCPVCRISYQPENIRP 69
Cdd:cd16743    3 CNICLETARDAVVSLCGHLFCWPCL---HQWLETRPERQECPVCKAGISRDKVIP 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-240 3.60e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 132 EEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASwKTQIQYDKTNVLADFEQLRDILDwEESNELQNLEKEEEDIL 211
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELE-ELEEELEELEEELEEAE 350

                         90       100
                 ....*....|....*....|....*....
gi 530395903 212 KSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEE 379
RING-HC_SHPRH-like cd16569
RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) ...
 14-60 3.64e-03

RING finger, HC subclass, found in SNF2 histone-linker PHD finger RING finger helicase (SHPRH) and similar proteins; SHPRH is a yeast RAD5 homolog found in mammals. It functions as an E3 ubiquitin-protein ligase that associates with proliferating cell nuclear antigen (PCNA), RAD18, and the ubiquitin-conjugating enzyme UBC13 (E2), and suppresses genomic instability by proliferating methyl methanesulfonate (MMS)-induced PCNA polyubiquitination. SHPRH contains a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a linker histone domain (H15), a PHD-finger, and a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA. This subfamily also includes tripartite motif-containing protein 15 (TRIM15). TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438231 [Multi-domain]  Cd Length: 53  Bit Score: 35.78  E-value: 3.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  14 TCPICLELLTQPLS-LDCGHSFCQACLTANHKKSMLDKGES-SCPVCRI 60
Cdd:cd16569    3 PCPICARPLGKQWSvLPCGHCFCLECIAILIDQYAQSRRRSlKCPICRE 51
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
 15-59 3.69e-03

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 35.41  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  15 CPICLE-LLTQPLSLDCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:cd23130    3 CPICLDdPEDEAITLPCLHQFCYTCILRWLQTS------PTCPLCK 42
RING-H2_Pirh2-like cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
 15-59 3.69e-03

RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It preferably ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits the transcriptional activity of p73, a homolog of the tumor suppressor p53, by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. It interacts with TIP60 and this association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to the Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs. This subfamily also includes Drosophila melanogaster Deltex, a ubiquitously expressed cytoplasmic ubiquitin E3 ligase that mediates Notch activation in Drosophila. It selectively suppresses T-cell activation through degradation of a key signaling molecule, MAP kinase kinase kinase 1 (MEKK1). It also inhibits Jun-mediated transcription at the stage of Ras-dependent Jun N-terminal protein kinase (JNK) activation. Deltex contains N-terminal two Notch-binding WWE domains that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a RING finger at the C-terminus.


Pssm-ID: 438127 [Multi-domain]  Cd Length: 45  Bit Score: 35.33  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903  15 CPICLELL---TQPLS-LDCGHSFCQACLtanhkKSMLDKGESSCPVCR 59
Cdd:cd16464    2 CPVCLEDLftsREPVHvLPCGHLMHSTCF-----EEYLKSGNYRCPLCS 45
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
 15-59 3.81e-03

RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway.


Pssm-ID: 438134 [Multi-domain]  Cd Length: 46  Bit Score: 35.30  E-value: 3.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLT--QPLSLDCGHSFCQACLTANHKKSmlDKGESSCPVCR 59
Cdd:cd16471    2 CPICLCAFKgrKCTLLSCSHVFHEACLSAFEKFI--ESKNQKCPLCR 46
mRING-HC-C3HC3D_Roquin2 cd16782
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-2; Roquin-2, also known as ...
 11-46 4.10e-03

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-2; Roquin-2, also known as membrane-associated nucleic acid-binding protein (MNAB), RING finger and CCCH-type zinc finger domain-containing protein 2 (RC3H2), or RING finger protein 164 (RNF164), is an E3 ubiquitin ligase that is localized to the cytoplasm and upon stress, is concentrated in stress granules. It is required for reactive oxygen species (ROS)-induced ubiquitination and degradation of apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5). Roquin-2 interacts with the 3'UTR of tumor necrosis factor receptor superfamily member 4 (TNFRSF4) and tumor-necrosis factor-alpha (TNFalpha), and modulates immune responses. Moreover, Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Roquin-2 contains an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 ubiquitin-ligase function, a highly conserved ROQ domain required for RNA binding and localization to stress granules, a coiled-coil (CC1), and a CCCH-type zinc finger that is involved in RNA recognition.


Pssm-ID: 438437  Cd Length: 49  Bit Score: 35.45  E-value: 4.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530395903  11 EEVTCPICL----ELLTQPLSLDCGHSFCQACLTANHKKS 46
Cdd:cd16782    4 EFLSCPICYnefdENVHKPISLGCSHTVCKTCLNKLHRKA 43
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
11-59 4.19e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 35.43  E-value: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530395903   11 EEVTCPICLELLTQPLSLDCGH-SFCQACLTanhkksMLDKGESSCPVCR 59
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHlCLCEECAE------RLLRKKKKCPICR 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
130-240 5.10e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  130 LTEEVAReyqvkLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNV--------LADFEQLRDILDwEESNELQ 201
Cdd:COG4913   615 LEAELAE-----LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereIAELEAELERLD-ASSDDLA 688

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530395903  202 NLEKEeediLKSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG4913   689 ALEEQ----LEELEAELEELEEELDELKGEIGRLEKELE 723
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
 15-61 5.72e-03

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in the degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 438119 [Multi-domain]  Cd Length: 44  Bit Score: 34.73  E-value: 5.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  15 CPICLELLTQPLSLDCGHSFCQACLtanhkKSMLDKGeSSCPVCRIS 61
Cdd:cd16455    3 CAICWESMQSARKLPCGHLFHNSCL-----RSWLEQD-TSCPTCRMS 43
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 6-69 5.89e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 38.14  E-value: 5.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530395903   6 LVNVKEEVTCPICLELLTQPLSLDCGHSFCQACL-----TANHKKSMLDKGE-----SSCPVCRISYQPENIRP 69
Cdd:PLN03208  12 LVDSGGDFDCNICLDQVRDPVVTLCGHLFCWPCIhkwtyASNNSRQRVDQYDhkrepPKCPVCKSDVSEATLVP 85
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-262 5.99e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903   132 EEVAREYQVKLQAALEMLRQKQQEAEELE---ADIREEKASWKTQIQYDkTNVLADFEQLRDIL-----DWEESneLQNL 203
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEkkhQQLCEEKNALQEQLQAE-TELCAEAEEMRARLaarkqELEEI--LHEL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530395903   204 E---KEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQgVDGVIKRTENVTL 262
Cdd:pfam01576   81 EsrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVT-TEAKIKKLEEDIL 141
Bbox2_TRIM65_C-IV cd19835
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65) and similar ...
 95-133 6.12e-03

B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65) and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.


Pssm-ID: 380893 [Multi-domain]  Cd Length: 42  Bit Score: 34.71  E-value: 6.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530395903  95 CARHGEKLLLFCQEDGKVICWLCErSQEHRGHHTFLTEE 133
Cdd:cd19835    3 CQRHGRPLELYCRTEKRCVCCKCT-VKECRNHNRVLLEE 40
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
 14-59 6.20e-03

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 34.64  E-value: 6.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530395903  14 TCPICLELLTQ-PLSLDCGHSFCQACLtanhkKSMLDKgESSCPVCR 59
Cdd:cd16479    3 TCIICREEMTVgAKKLPCGHIFHLSCL-----RSWLQR-QQTCPTCR 43
RING-HC_SH3RF1 cd16748
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and ...
 15-59 6.23e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. It also plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and c-Jun N-terminal kinase (JNK) mediated apoptosis, linking Rac1 to downstream components. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. Moreover, SH3RF1 assembles an inhibitory complex with the actomyosin regulatory protein Shroom3, which links to the actin-myosin network to regulate neuronal process outgrowth. It also forms a complex with apoptosis-linked gene-2 (ALG-2) and ALG-2-interacting protein (ALIX/AIP1) in a calcium-dependent manner to play a role in the regulation of the JNK pathway. Furthermore, direct interaction of SH3RF1 and another molecular scaffold JNK-interacting protein (JIP) is required for apoptotic activation of JNKs. Interaction of SH3RF1 and E3 ubiquitin-protein isopeptide ligases, Siah proteins, further promotes JNK activation and apoptosis. In addition, SH3RF1 binds to and degrades TAK1, a crucial activator of both the JNK and the Relish signaling pathways. SH3RF1 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438406 [Multi-domain]  Cd Length: 48  Bit Score: 34.99  E-value: 6.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530395903  15 CPICLELLTQPLS-LDCGHSFCQACLTAnhkkSMLDKGESSCPVCR 59
Cdd:cd16748    5 CPVCLERLDATAKvLPCQHTFCRRCLLG----IVGSRSELRCPECR 46
mRING-HC-C3HC3D_PHRF1 cd16635
Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger ...
 11-62 6.88e-03

Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger domain-containing protein 1 (PHRF1) and similar proteins; PHRF1, also known as KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase which induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438297 [Multi-domain]  Cd Length: 51  Bit Score: 34.70  E-value: 6.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530395903  11 EEVTCPICL-ELLTQPLSL--DCGHSFCQACLTANHKKSmldkgeSSCPVCRISY 62
Cdd:cd16635    3 ESESCPICLnTFRDQAVGTpeSCDHIFCLDCILEWSKNA------NTCPVDRIVF 51
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
120-247 7.20e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 120 SQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIRE---EKASWKTQIqydktnvladfEQLRDILDWEE 196
Cdd:COG4717  122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEleaELAELQEEL-----------EELLEQLSLAT 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530395903 197 SNELQNLEKEEEDILKSLTNSETEMvqqtQSLRELISDLEHRLQGSVMELL 247
Cdd:COG4717  191 EEELQDLAEELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELE 237
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
142-261 7.35e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 142 LQAALEMLRQKQQEAEELEADIREEKASwKTQIQydktnvladfEQLRdildwEESNELQNLEKEEEDILKSLTNSETEM 221
Cdd:COG4372   33 LRKALFELDKLQEELEQLREELEQAREE-LEQLE----------EELE-----QARSELEQLEEELEELNEQLQAAQAEL 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530395903 222 VQQTQSLRELISDLEhRLQGSVMELLQGVDGVIKRTENVT 261
Cdd:COG4372   97 AQAQEELESLQEEAE-ELQEELEELQKERQDLEQQRKQLE 135
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
130-246 7.61e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 130 LTEEVAREYQVKLQAALEMLRQKQQEAEELeadiREEKASWKTQIQYDKTNVLADFEQLRDI---------LDWEESNEL 200
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQA----REELEQLEEELEQARSELEQLEEELEELneqlqaaqaELAQAQEEL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530395903 201 QNLEKEEEDI---LKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMEL 246
Cdd:COG4372  104 ESLQEEAEELqeeLEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
 12-40 8.45e-03

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promotes the degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates the activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 438296 [Multi-domain]  Cd Length: 43  Bit Score: 34.32  E-value: 8.45e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 530395903  12 EVTCPICLELLTQPLSL-DCGHSFCQACLT 40
Cdd:cd16634    1 ELICPICSGVLEEPLQApHCEHAFCNACIT 30
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 135-242 9.12e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 37.67  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903  135 AREYQVKLQAALEMLRQKQQEAEELEADIREEKASwktqiQYDKTnvlaDFEQLRDILDwEESNELQNLEKEEEDILKSL 214
Cdd:pfam12795  39 AAAYQKALDDAPAELRELRQELAALQAKAEAAPKE-----ILASL----SLEELEQRLL-QTSAQLQELQNQLAQLNSQL 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 530395903  215 TNSET--EMVQQTQS-LRELISDLEHRLQGS 242
Cdd:pfam12795 109 IELQTrpERAQQQLSeARQRLQQIRNRLNGP 139
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-240 9.24e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530395903 131 TEEVAREYQVKLQAALEMLRQKQQEA----EELEADIREEKASwKTQIQYDKTNVLADFEQLRDILDwEESNELQNLEKE 206
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELelelEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLE-ELEEELAELEEE 331

                         90       100       110
                 ....*....|....*....|....*....|....
gi 530395903 207 EEDILKSLTNSETEMVQQTQSLRELISDLEHRLQ 240
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
 9-39 9.28e-03

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438378 [Multi-domain]  Cd Length: 47  Bit Score: 34.19  E-value: 9.28e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 530395903   9 VKEEVTCPICLELLTQPLSLDCGHSFCQACL 39
Cdd:cd16718    1 VDPDFKCNLCNKVLEDPLTTPCGHVFCAGCV 31
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
 14-59 9.68e-03

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; This family includes two highly similar E3 ubiquitin-protein ligases, Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in the brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Praja-1 also regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of Dlxin-1, via a ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP)-dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, it forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 438128 [Multi-domain]  Cd Length: 46  Bit Score: 34.35  E-value: 9.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530395903  14 TCPICL------ELLTQplsLDCGHSFCQACLTANHKKSmldkgeSSCPVCR 59
Cdd:cd16465    1 CCPICCseyvkdEIATE---LPCHHLFHKPCITAWLQKS------GTCPVCR 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH